1. Curriculum Vitae (Professor Mark Carr)
Personal Information
Name: Mark David Carr
Date of Birth: 20th
September 1961
Present Position: Professor of Biochemistry and Director of Enterprise for the College of
Medicine, Biological Sciences and Psychology
Contact Details: Department of Biochemistry, College of Medicine, Biological Sciences and
Psychology, University of Leicester, Henry Wellcome Building, Lancaster
Road, Leicester, LE1 9HN, UK
E.mail: mdc12@le.ac.uk Tel: 0116 229 7075 Fax: 0116 229 7018
Qualifications: D.Phil. Biochemistry, University of Oxford, 1987
B.Sc. Hons. Biochemistry, Class 2:1, University of Birmingham, 1983
Brief Employment History
2001-09 Reader in Biological NMR Spectroscopy, Department of Biochemistry, University of
Leicester, UK.
1997-01 Lecturer in Structural Biology, Department of Biosciences, University of Kent, UK.
1993-97 Group Leader, Laboratory of Molecular Structure, National Institute for Biological
Standards and Control, London, UK.
1989-93 MRC Postdoctoral Fellow, Laboratory of Molecular Structure, National Institute for
Medical Research, London, UK.
1987-89 Royal Society Postdoctoral Fellow and Max-Planck-Society Postdoctoral Fellow,
Max-Planck-Institute for Medical Research, Heidelberg, Germany.
Research Activities and Interests
I have maintained and managed a successful research group for over 20 years, which
currently contains 3 postdoctoral scientists, a research technician and 5 Ph.D students. My
scientific career has concentrated on determining the structures, functions, interactions and
mechanisms of action of proteins and protein complexes involved in key biological processes of
significant medical importance, which remains a major focus of my laboratory. The ongoing
research in my group aims to integrate the information obtained from molecular, cellular and
structural biology-based approaches to provide a detailed understanding of the function of proteins
involved in disease states. In addition, through close collaboration with pharmaceutical companies
such as UCB-Celltech and translational charities such as MRC Technology, we aim to make a
major contribution to the discovery and development of important new drugs, such as therapeutic
antibodies targeted at secreted signalling proteins. Current research within my group falls into four
main areas, which are outlined below.
i) Structural Biology in Drug Discovery and Development. High resolution structural
information for proteins, functional protein complexes and protein-ligand complexes now plays a
major role in the discovery, development and patent protection of new therapeutic molecules. In
close collaboration with groups at UCB-Celltech and MRC Technology we are using NMR and X-
ray-based methods to determine the structures of promising new protein and protein complex drug
targets, to map the binding sites for natural regulators and candidate drugs, and to determine the
orientations and conformations of potential drugs bound to target proteins. This approach has
proved to be highly successful and informative for both traditional small molecules and for a wide

2. range of potential therapeutic antibodies. We are also developing new, improved and more rapid
NMR-based approaches to obtain detailed structural information for large protein-protein and
protein-drug complexes (50-100 kDa).
ii) Structures, Interactions and Mechanisms of Action of Protein Regulators of Wnt
Signalling: The canonical Wnt signalling pathway has emerged as a key regulator of bone growth
and remodelling, with activation of the pathway leading to the deposition of new bone and
increased bone density. Osteoporosis and related conditions occur as a consequence of the loss
of bone integrity, and represent a major and growing medical challenge across the world, with
current therapeutic interventions showing only limited success. The activation of Wnt signalling is
tightly regulated by a number of secreted proteins, including members of the Dickkopf family (Dkk-
1, Dkk-2, Dkk-3 and Dkk-4) and sclerostin (SOST), which share the ability to interact with
membrane-bound co-receptors for Wnt proteins (LRP5 and LRP6) leading to inhibition of Wnt
signalling. These natural regulatory systems, together with the central role of Wnt signalling in
bone homeostasis, highlight modulation of the regulation of Wnt signalling as an attractive target
for the development of effective therapeutics to treat osteoporosis. In collaboration with UCB
Celltech, current research in my group is focussed on characterising the structures and interactions
of key protein regulators of Wnt signalling, including Dkk and Kremen family proteins.
iii) Molecular Basis of Tuberculosis Pathogenesis. Tuberculosis remains one of the most
significant bacterial diseases of humans, with about one third of the world’s population infected
resulting in over 2 million deaths annually. Research in my group is focussed on determining the
structures, functions and mechanisms of action of secreted mycobacterial proteins and complexes
llinked to tuberculosis pathogenesis. This work is a collaboration with several colleagues at
Leicester.
iv) Molecular Basis of the Control of Eukaryotic Gene Expression. Control of eukaryotic
gene expression is dependent upon the assembly of a diverse range of protein-protein and protein-
nucleic acid complexes. The main focus of current work in my group is the highly conserved
protein Pdcd4, which has recently emerged as a key regulator of both transcription and translation,
mediated via specific protein-protein and protein-RNA interactions. The aim of ongoing work is to
determine the molecular basis of the cellular functions of Pdcd4, which should lead to a clearer
picture of the functions associated with its role as a tumour suppressor. This research forms part of
a successful and long-term collaboration with Prof. Karl-Heinz Klempnauer’s group at the
University of Münster.
Current Research Grants
My research group has current research funding of over £2.7 million and I was the sole or
principal applicant on all current grants apart from the joint BBSRC/MRC Technology funded Ph.D
studentship.
1. MRC Ph.D Studentship. Structural and functional characterisation of cytokine receptor-like
factor 2 (CRLF2) and development of novel cancer therapeutics. £79,765, 1.10.14-31.3.18
(jointly with Prof. Martin Dyer)
2. BBSRC/MRC Technology Ph.D Studentship. Structural and chemical biology approaches to
characterise protein-protein interactions that regulate kinases. £111,560, 1.10.14-30.9.18
(jointly with Prof. Richard Bayliss)
3. Commonwealth Ph.D Scholarship. Novel mechanisms of translational regulation by the N-
terminal region of the tumour suppressor protein programmed cell death protein 4 (Pdcd4).
£83,418, 1.10.14-30.9.17
4. BBSRC/UCB Pharma Ph.D Studentship. Structures, interactions and mechanisms of action
of secreted protein regulators of Wnt signalling: laying the foundations for future drug
discovery. £131,672, 1.10.12-30.9.16
5. MRC Technology Structural Biology Partnership Grant. Structure-based drug discovery
and development. £650,880, 1.3.12-31.12.16 (a rolling, open-ended grant funded for a
minimum of 2 further years, held jointly with Prof. Richard Bayliss)
6. UCB Pharma Collaborative Programme Grant. High field NMR studies of protein-drug
interactions. £1,335,786, 1.2.09-31.1.18 (a rolling, open-ended grant funded for a minimum of 2
further years)

3. 7. Malaysian Government Ph.D Studentship. Functions of secreted mycobacterial proteins in
tuberculosis pathogenesis. £95,940, 1.10.11-30.9.14
8. MRC/UCB Pharma Ph.D Studentship. Development of robust, reliable and rapid NMR-based
approaches to obtain high quality models for complexes formed between lead drug molecules
and target proteins: from fragment screens to therapeutic antibodies. £113,920, 1.10.10-
30.9.14
9. UCB Pharma Ph.D Studentship. NMR structure determination of camelid VHH antibodies.
£113,920, 1.10.10-30.9.14
10. BBSRC Ph.D Studentship. Mycobacterial resuscitation-promoting factors (Rpfs): roles and
mechanisms in infected macrophages. £71,920, 1.10.10-30.9.14 (jointly with Dr Galina
Mukamolova)
Other Research Activities
I have acted as a structural biology consultant for the major pharmaceutical company UCB-
Celltech for the last 12 years. I also regularly review grant applications (project, programme and
fellowships) for major biomedical funding organisations, such as the Wellcome Trust, Arthritis
Research Council and Medical Research Council. Similarly, I regularly review submitted papers for
several major international journals, including the Journal of Biological Chemistry. I have also acted
as an external assessor in the recruitment of several group leaders to Medical Research Council
Institutes and have played a major role in the recruitment and selection of new academic and
research staff at the University at Leicester. I have been the external examiner for Ph.D and M.Phil
students at the Universities of London (University College), Birmingham, Nottingham and Warwick.
Teaching Responsibilities
I make a full contribution to the design, development and delivery of both undergraduate
and postgraduate teaching in the College of Medicine, Biological Sciences and Psychology at
Leicester.
Administrative Duties
I have been the Director of Enterprise for the College of Medicine, Biological Sciences and
Psychology at Leicester for several years, which is a key leadership role in developing research
based enterprise activities. I chair the College Enterprise Committee, am a member of the College
Management Board and represent the College on the University Enterprise Committee.
For over 11 years I have been one of the Postgraduate Tutors in the Biochemistry
Department at Leicester, which currently has about 40 Ph.D students and over 50 M.Sc students. I
have taken a leading role in the College on Ph.D matters, including the successful introduction of
several new initiatives, such as the holding of an annual Postgraduate Careers Symposium.
Publications in International Journals
I have published 58 primary research papers in major peer-reviewed international journals.
Please note that the corresponding authors for papers are underlined.
1. Addis, P.W., Hall, C.J., Bruton, S., Veverka, V., Wilkinson, I.C., Muskett, F.W., Renshaw, P.S.,
Prosser, C.E., Carrington, B., Lawson, A.D.G., Griffin, R., Cain, K., Taylor, R.J., Waters, L.C.,
Henry, A.J. and Carr, M.D. (2014) Conformational heterogeneity in antibody-protein antigen
recognition: implications for high affinity protein complex formation. J. Biol. Chem. 289, 7200-
7210.
2. Barkell, A.M., Holdsworth, G., Waters, L.C., Veverka, V., Slocombe, P.M. Muskett, F.W.,
Henry, A.J., Robinson, M.K. and Carr, M.D. (2014) Resonance assignment and secondary
structure determination of full length human Dickkopf 4 (hDkk4), a secreted, disulphide-rich
Wnt inhibitor protein. Biomol. NMR Assign. DOI 10.1007/s12104-014-9562-2

4. 3. Bortoluzzi, A., Muskett, F.W., Waters, L.C., Addis, P.W., Rieck, B., Munder, T., Schleier, S.,
Forti, F., Ghisotti, D., Carr, M.D. and O’Hare H.M. (2013) Mycobacterium tuberculosis RNA
polymerase-binding protein A (RbpA) and its interactions with sigma factors. J. Biol. Chem.
288, 14438-14450.
4. Prosser, C.E., Waters, L.C., Muskett, F.W., Veverka, V., Addis, P.W., Griffin, L.M., Baker, T.S.,
Lawson, A.D.G., Wernery, U., Kinne, J., Henry, A.J., Taylor, R.J. and Carr, M.D. (2013) 15
N,
13
C and 1
H resonance assignments and secondary structure determination of a variable heavy
domain of a heavy chain antibody. Biomol. NMR Assign. doi 10.1007/s 12104-013-9464-8.
5. Lightwood, D., O’Dowd, V., Carrington, B., Veverka, V., Carr, M.D., Tservistas, M., Henry, A.J.,
Smith, B., Tyson, K., Lamour, S., Sarkar, K., Turner, A., Lawson, A.D., Bourne, T., Gozzard, N.
and Palframan, R. (2013) The discovery, engineering and characterisation of a highly potent
anti-human IL-13 Fab fragment designed for administration by inhalation. J. Mol. Biol. 425,
577-593.
6. Structure and interactions of the human programmed cell death 1 receptor. Cheng, X.,
Veverka, V., Radhakrishnan, A., Waters, L.C., Muskett, F.W., Morgan, S., Lesley, A., Griffiths,
M., Stubberfield, C., Griffin, R., Henry, A.J., Jansson, A., Ladbury, J.E., Ikemizu, S., Carr, M.D.
and Davis, S.J. (2013) J. Biol. Chem. 288, 11771-11785.
7. Kumar, N., Wethkamp, N., Waters, L.C., Carr, M.D. and Klempnauer, K.H. (2013) Tumor
suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the
Hipk2-dependent phosphorylation of p53 at serine 46. Oncogenesis 2, e37; doi:10.1038/
oncsis2012.37.
8. Oka, O., Waters, L.C., Strong, S.L., Dosanjh, N.S., Veverka, V., Muskett, F.W., Renshaw, P.S.,
Klempnauer, K.H. and Carr, M.D. (2012) Interaction of the transactivation domain of B-Myb
with the TAZ2 domain of the coactivator p300: molecular features and properties of the
complex. PLoS ONE 7 (12), e52906.
9. Veverka, V., Baker, T., Redpath, N.T., Carrington, B., Muskett, F.W., Lawson, A.D.G., Taylor,
R.J., Henry, A.J., and Carr, M.D. (2012) Conservation of functional sites on interleukin-6 and
implications for evolution of signaling complex assembly and therapeutic intervention. J. Biol.
Chem. 287, 40043-40050.
10. Holdsworth, G., Slocombe, P., Doyle, C., Sweeney, B., Veverka, V., Le Riche, K., Franklin,
R.J., Compson, J., Brookings, D., Turner, J., Kennedy, J., Garlish, R., Shi, J., Newnham, L.,
McMillan D., Muzylak, M., Carr, M.D., Henry, A.J., Ceska, T. and Robinson M.K. (2012)
Characterisation of the interaction of sclerostin with the low density lipoprotein receptor-related
protein (LRP) family of Wnt co-receptors. J. Biol. Chem. 287, 26464-26477.
11. Illingworth, C.J.R., Chintipalli, S.V., Serapian, S.A., Miller, A.D., Veverka, V., Carr, M.D. and
Reynolds, C.A. (2012) The statistical significance of selected sense-antisense peptide
interactions. J. Comp. Chem. 33, 1440-1447.
12. Ilghari, D., Lightbody K.L., Veverka, V., Waters, L.C., Muskett, F.W., Renshaw, P.S. and Carr,
M.D. (2011) Solution structure of the M. tuberculosis EsxG.EsxH complex: functional
implications and comparisons with other M. tuberculosis Esx family complexes. J. Biol. Chem.
286, 29993-30002.
13. Waters, L.C., Strong, S.L., Ferlemann, E., Ojore, O., Muskett, F.W., Veverka, V., Banerjee, S.,
Schmedt, T., Henry, A.J., Klempnauer, K.-H. and Carr, M.D. (2011) Structure of the tandem
MA-3 region of Pdcd4 and characterisation of its interactions with eIF4A and eIF4G: molecular
mechanisms of a tumour suppressor. J. Biol. Chem. 286, 17270-17280.

5. 14. Singh, P., Wedeken, L., Waters, L.C., Carr, M.D. and Klempnauer, K.-H. (2011) Pdcd4 directly
binds the coding region of c-myb mRNA and suppresses its translation. Oncogene 30, 4864-
4873.
15. Waters, L.C., Oka, O., Muskett, F.W., Strong, S.L., Schmedt, T., Klempnauer, K.-H. and Carr,
M.D. (2010) Resonance assignment and secondary structure of the middle MA-3 domain and
complete tandem MA-3 region of the tumour suppressor protein Pdcd4. Biomol. NMR Assign.
4, 49-53.
16. Wilkinson, I.C., Hall, C.J., Veverka, V., Shi, J.Y., Muskett, F.W., Stephens, P.E., Taylor, R.J.,
Henry, A.J. and Carr, M.D. (2009) High resolution NMR-based model for the structure of a
scFv-IL-1β complex: potential for NMR as a key tool in therapeutic antibody design and
development. J. Biol. Chem. 284, 31928-31935.
17. Ilghari, D., Waters, L.C., Veverka, V., Muskett, F.W. and Carr, M.D. (2009) 15
N, 13
C and 1
H
resonance assignments and secondary structure determination of the Mycobacterium
tuberculosis Rv0287-Rv0288 protein complex. Biomol. NMR Assign.. 3, 171-174.
18. Veverka, V., Henry, A.J., Slocombe, P.M., Ventom, A., Mulloy, B., Muskett, F.W., Muzylak, M.,
Greenslade, K., Moore, A., Zhang, L., Gong, J., Qian, X., Paszty, C., Taylor, R.J., Robinson,
M.K. and Carr, M.D. (2009) Characterization of the structural features and interactions of
sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. J. Biol.
Chem. 284, 10890-10900.
19. Lightbody, K.L., Ilghari, D., Waters, L.C., Carey, G., Bailey, M.A., Williamson, R.A., Renshaw,
P.S. and Carr, M.D. (2008) Molecular features governing the stability and specificity of
functional complex formation by Mycobacterium tuberculosis CFP-10/ESAT-6 family proteins.
J. Biol. Chem. 283, 17681-17690.
20. Veverka, V., Crabbe, T., Bird, I., Lennie, G., Muskett, F.W., Taylor, R.J. and Carr, M.D. (2008)
Structural characterization of the interaction of mTOR with phosphatidic acid and a novel class
of inhibitor: compelling evidence for a central role of the FRB domain in small molecule-
mediated regulation of mTOR. Oncogene 27, 585-595.
21. Waters, L.C., Veverka, V., Böhm, M., Schmedt, T., Choong, P.T., Muskett, F.W., Klempnauer,
K.-H. and Carr, M.D. (2007) Structure of the C-terminal MA-3 domain of the tumour
suppressor protein Pdcd4 and characterisation of its interaction with eIF4A. Oncogene 26,
4941-4950.
22. Waters, L., Yue, B., Veverka, V., Renshaw, P., Bramham, J., Matsuda, S., Frenkiel, T., Kelly,
G., Muskett, F.W., Carr, M.D. and Heery, D.M. (2006) Structural diversity in p160/CREB-
binding protein coactivator complexes. J. Biol. Chem. 281, 14787-14795.
23. Waters, L.C., Böhm, M., Veverka, V., Muskett, F.W., Frenkiel, T.A., Kelly, G.P., Prescott, A.,
Dosanjh, N.S., Klempnauer, K.-H. and Carr, M.D. (2006) NMR assignment and secondary
structure determination of the C-terminal MA-3 domain of the tumour suppressor protein
Pdcd4. J. Biomol. NMR 36, S5, 18.
24. Veverka, V., Gregor, L., Crabbe, T., Bird, I., Taylor, R.J. and Carr, M.D. (2006) Letter to the
Editor: NMR assignment of the mTOR domain responsible for rapamycin binding. J. Biomol.
NMR 36, S5, 3.
25. Renshaw, P.S., Lightbody, K.L., Veverka, V., Muskett, F.W., Kelly, G., Frenkiel, T.A., Gordon,
S.V., Hewinson, R.G., Burke, B., Norman, J., Williamson, R.A. and Carr, M.D. (2005) Structure
and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6.
EMBO J. 24, 2491-2498.

6. 26. Marei, A., Ghaemmaghami, A., Renshaw, P., Wiselka, M., Barer, M., Carr, M.D. and Ziegler-
Heitbrock, L. (2005) Superior T cell activation by ESAT-6 as compared with the ESAT-6·CFP-
10 complex. Int. Immunol. 17, 1439-1446.
27. Lightbody, K.L., Renshaw, P.S., Collins, M.L., Wright, R.L., Hunt, D.M., Gordon, S.V.,
Hewinson, R.G., Buxton R.S., Williamson, R.A. and Carr, M.D. (2004) Characterisation of
complex formation between members of the Mycobacterium tuberculosis complex CFP-
10/ESAT-6 protein family; towards an understanding of the rules governing complex formation
and thereby functional flexibility. FEMS Microbiol. Lett. 238, 255-262.
28. Renshaw, P.S., Veverka, V., Kelly, G., Frenkiel, T.A., Williamson, R.A., Gordon, S.V.,
Hewinson, R.G. and Carr, M.D. (2004) Letter to the Editor: Sequence-specific assignment and
secondary structure determination of the 195-residue complex formed by the Mycobacterium
tuberculosis proteins CFP-10 and ESAT-6: Towards an understanding of their role in
tuberculosis pathogenesis. J. Biomol. NMR 30, 225-226.
29. Carr, M.D., Bloemink, M.J., Dentten, E., Whelan, A.O., Gordon, S.V., Kelly, G., Frenkiel, T.A.,
Hewinson, R.G. and Williamson, R.A. (2003) Solution structure of the Mycobacterium
tuberculosis complex protein MPB70: from tuberculosis pathogenesis to inherited human
corneal disease. J. Biol. Chem. 278, 43736-43743.
30. Jones, G., Howard, M., McIntosh, P., Williamson, R.A. and Carr, M.D. (2003) Letter to the
Editor: Sequence-specific assignment of the B-Myb DNA-binding domain (B-MybR2R3) bound
to a 16 base-pair DNA target site corresponding to a regulatory site from the tom-1 gene. J.
Biomol. NMR 26, 375-376.
31. Renshaw, P.S., Panagiotidou, P., Whelan, A., Gordon, S.V., Hewinson, R.G., Williamson, R.A.
and Carr, M.D. (2002) Conclusive evidence that the major T-cell antigens of the M. tuberculosis
complex ESAT-6 and CFP-10 form a tight, 1:1 complex and characterisation of the structural
properties of ESAT-6, CFP-10 and the ESAT-6-CFP-10 complex: implications for pathogenesis
and virulence. J. Biol. Chem. 277, 21598-21603.
32. Williamson, R.A., Hutton, M., Vogt, G., Rapti, M., Knauper, V., Carr, M.D. and Murphy, G.
(2001) Tyrosine 36 plays a critical role in the interaction of the AB loop of TIMP-2 with matrix
metalloproteinase-14. J. Biol. Chem. 276, 32966-32970.
33. Lemercinier, X., Muskett, F.W., Cheeseman, B., McIntosh, P.B., Thim, L. and Carr M.D. (2001)
High resolution solution structure of human intestinal trefoil factor and functional insights from
detailed structural comparisons with the other members of the trefoil family of cell motility
factors. Biochemistry 40, 9552-9559.
34. Bloemink, M.J., Kemmink, J., Dentten, E., Muskett, F.W., Whelan, A., Sheikh, A., Hewinson,
G., Williamson, R.A. and Carr, M.D. (2001) Sequence-specific assignment and determination
of the secondary structure of the 163 residue M. tuberculosis and M. bovis antigenic protein
mpb70. J. Biomol. NMR 20, 185-186.
35. Williamson, R.A., Muskett, F.W., Howard, M.J., Freedman, R.B. and Carr, M.D. (1999) The
effect of matrix metalloproteinase complex formation on the conformational mobility of tissue
inhibitor of metalloproteinases-2 (TIMP-2). J. Biol. Chem. 274, 37226-37232.
36. Muskett, F.W., Frenkiel, T.A., Feeney, J., Freedman, R.B., Carr, M.D. and Williamson, R.A.
(1998) High resolution structure of the N-terminal domain of tissue inhibitor of
metalloproteinases-2 and characterisation of its interaction site with matrix metalloproteinase-3.
J. Biol. Chem. 273, 21736-21743.
37. McIntosh, P.B., Frenkiel, T.A., Wollborn, U., McCormick, J.E., Klempnauer, K.-H., Feeney, J.
and Carr, M.D. (1998). Solution structure of the B-Myb DNA-binding domain: a possible role for

7. conformational instability of the protein in DNA-binding and control of gene expression.
Biochemistry 37, 9619-9629.
38. Bloch, C., Patel, S.U., Baud, F., Zvelebil, M., Carr, M.D., Sadler, P. and Thornton, J.M. (1998)
1
H NMR structure of an antifungal -thionin protein SI1: similarity to scorpion toxins. Proteins:
Struct. Funct. Genet. 32, 334-349.
39. Williamson, R.A., Carr, M.D., Frenkiel, T.A., Feeney, J. and Freedman, R.B. (1997) Mapping
the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of
metalloproteinase-2 by NMR chemical shift perturbation. Biochemistry 36, 13882-13889.
40. Carr, M.D., Wollborn, U., McIntosh, P.B., Frenkiel, T.A., McCormick, J.E., Bauer, C.J.,
Klempnauer, K.-H. and Feeney, J. (1996) Structure of the B-Myb DNA-binding domain in
solution and evidence for multiple conformations in the region of repeat-2 involved in DNA-
binding: implications for sequence-specific DNA-binding by Myb proteins. Eur. J. Biochem. 235,
721-735.
41. Williamson, R.A., Natalia, D., Gee, C.K., Murphy, G., Carr, M.D. and Freedman, R.B. (1996)
Chemically and conformationally authentic active domain of human tissue inhibitor of
metalloproteinases-2 refolded from bacterial inclusion bodies. Eur. J. Biochem. 241, 476-483.
42. Polshakov, V.I., Frenkiel, T.A., Westley, B., Chadwick, M., May, F., Carr, M.D. and Feeney, J.
(1995) NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide.
Similarities to porcine spasmolytic peptide (pSP) and evidence for a monomeric structure. Eur.
J. Biochem. 233, 847-855.
43. Williamson, R.A., Martorell, G., Carr, M.D., Murphy, G., Docherty, A.J.P., Freedman, R.B. and
Feeney, J. (1994). Solution structure of the active domain of tissue inhibitor of
metalloproteinases-2. A new member of the OB fold protein family. Biochemistry 33, 11745-
11759.
44. Carr, M.D., Bauer, C.J., Gradwell, M.J. and Feeney, J. (1994). Solution structure of a trefoil-
motif-containing cell growth factor, porcine spasmolytic protein. Proc. Natl. Acad. Sci. U.S.A.
91, 2206-2210.
45. De, A., Brown, D.G., Gorman, M.A., Carr, M.D., Sanderson, M.R. and Freemont, P.S. (1994).
Crystal structure of a disulfide-linked trefoil motif found in a large family of putative growth
factors. Proc. Natl. Acad. Sci. U.S.A. 91, 1084-1088.
46. Soteriou, A., Carr, M.D., Frenkiel, T.A., McCormick, J.E., Bauer, C.J., Sali, D., Birdsall, B. and
Feeney, J. (1993). 3D 13
C/1
H NMR-based assignments for side-chain resonances of
Lactobacillus casei dihydrofolate reductase. Evidence for similarities between the solution and
crystal structures of the enzyme. J. Biomol. NMR 3, 535-546.
47. Ostler, G., Soteriou, A., Moody, C.M., Khan, J.A., Birdsall, B., Carr, M.D., Young, D. and
Feeney, J. (1993). Stereospecific assignments of the leucine methyl resonances in the 1
H
nuclear magnetic resonance spectrum of L.casei dihydrofolate reductase. FEBS Lett. 318, 177-
180.
48. Soteriou, A., Carr, M.D., Frenkiel, T.A., Bauer, C.J., McCormick, J.E., Birdsall, B. and Feeney,
J. (1993). Essentially complete 13
C, 15
N and 1
H resonance assignments for the methotrexate
complex of Lactobacillus casei dihydrofolate reductase, based on isotopic labelling of the
protein with 2
H, 13
C and 15
N and multidimensional NMR spectroscopy. J. Cell. Biochem. 17,
285.
49. Carr, M.D. (1992). 1
H NMR-based determination of the secondary structure of porcine
pancreatic spasmolytic polypeptide: one of a new family of trefoil motif containing cell growth

8. factors. Biochemistry 31, 1998-2004.
50. Carr, M.D. and Mott, R.F. (1991). The transcriptional control proteins c-Myb and v-Myb contain
a basic region DNA binding motif. FEBS Lett. 282, 293-294.
51. Carr, M.D., Birdsall, B., Frenkiel, T.A., Bauer, C.J., Jimenez-Barbero, J., Polshakov, V.I.,
McCormick, J.E., Roberts, G.C.K. and Feeney, J. (1991). Dihydrofolate reductase: sequential
resonance assignments using 2D and 3D NMR and secondary structure determination in
solution. Biochemistry 30, 6330-6341.
52. Feeney, J., Bauer, C.J., Frenkiel, T.A., Birdsall, B., Carr, M.D., Roberts, G.C.K. and Arnold,
J.R.P. (1991). Deceptively simple exchange effects in homonuclear Hartmann-Hahn
(HOHAHA) spectra of protein-ligand complexes. J. Magn. Reson. 91, 607-613.
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