Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces

Protein Science

Volumn 13, Issue 5, 2004, Pages 1238-1250

  O'Leary, Joanne M ^a,b   Bromek, Krystyna ^a   Black, Gordon M ^a   Uhrinova, Stanislava ^a   Schmitz, Christian ^a,c   Wang, Xuefeng ^a,d   Krych, Malgorzata ^a,d   Atkinson, John P ^a,d   Uhrin, Dusan ^a   Barlow, Paul N ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF HEIDELBERG   (Germany)

^d WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Backbone dynamics; CCP module; Complement; NMR; SCR

Indexed keywords

COMPLEMENT COMPONENT C3B RECEPTOR; COMPLEMENT CONTROL PROTEIN; MEMBRANE COFACTOR PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANTIGENS, CD; ANTIGENS, CD46; COMPLEMENT ACTIVATION; CONSENSUS SEQUENCE; MEMBRANE GLYCOPROTEINS; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; RECEPTORS, COMPLEMENT 3B; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 11144357078     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03582704     Document Type: Article

References (50)

1. 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31: 5269-5278.
2. Barlow, P.N., Steinkasserer, A., Norman, D.G., Kieffer, B., Wiles, A.P., Sim, R.B., and Campbell, I.D. 1993. Solution structure of a pair of complement modules by nuclear magnetic resonance. J. Mol. Biol. 232: 268-284.
3. Birmingham, D.J. and Hebert, L.A. 2001. CR1 and CR1-like: The primate immune adherence receptors. Immunol. Rev. 180: 100-111.
4. Bork, P., Downing, A.K., Kieffer, B., and Campbell, I.D. 1996. Structure and distribution of modules in extracellular proteins. Q. Rev. Biophys. 29: 119-167.
5. Bramham, J., Hodgkinson, J.L., Smith, B.O., Uhrin, D., Barlow, P.N., and Winder, S. 2002. Solution structure of the calponin CH domain and fitting to the helical reconstruction of F-actin:calponin. Structure 10: 249-258.
6. Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.-S., Kuszewski, J., Nilges, N., Pannu, N.S., et al. 1998. Crystallography and NMR system (CNS): A new software system for macromolecular structure determination. Acta Crystallogr. D 54: 905-921.
7. Casasnovas, J.M., Larvie, M., and Stehle, T. 1999. Crystal structure of two CD46 domains reveals an extended measles virus-binding surface. EMBO J. 18: 2911-2922.
8. Crump, M.P., Spyracopoulos, L., Lavigne, P., Kim, K.S., Clark-Lewis, I., and Sykes, B.D. 1999. Backbone dynamics of the human CC chemokine eotaxin: Fast motions, slow motions, and implications for receptor binding. Protein Sci. 8: 2041-2054.
9. de la Torre, J.G., Huertas, J., and Carrasco, B. 2000. Calculation of hydrodynamic properties of proteins from their atomic structure. Biophys. J. 78: 719-730.
10. Duggan, B.M., Dyson, H.J., and Wright, P.E. 1999. Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2. Eur. J. Biochem. 2: 539-548.
11. 125I-human C3b, the third component of complement, to specific receptors in human cultured B lymphoblastoids cells: Characterization of a low affinity interaction. J. Immunol. 125: 1332-1339.
12. Griswold, I.J. and Dahlquist, F.W. 2002. The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: Implications for potential protein-protein interaction sites. Biophys. Chem. 101-102: 359-373.
13. Henderson, C., Bromek, K., Smith, B.O., Uhrin, D., and Barlow, P.N. 2001. Structure and dynamics of the central modules of a poxvirus complement control protein. J. Mol. Biol. 307: 323-339.
14. Herbert, A., O'Leary, J., Krych-Goldberg, M., Atkinson, J.P., and Barlow, P.N. 2002. Three-dimensional structure and flexibility of proteins of the RCA family: A progress report. Biochem. Soc. Trans. 30: 990-996.
15. Hsu, E.C., Sabatinos, S., Hoedemaeker, F.J., Rose, D.R., and Richardson, C.D. 1999. Use of site-specific mutagenesis and monoclonal antibodies to map regions of CD46 that interact with measles virus H protein. Virology 258: 314-326.
16. 13CO-relaxation measurements. Biochemistry 38: 10567-10577.
17. Ishima, R. and Torchia, D.A. 2000. Protein dynamics from NMR. Nat. Struct. Biol. 7: 740-743.
18. 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease. Biochemistry 28: 8972-8979.
19. 2 values in proteins. J. Magn. Reson. 97: 359-375.
20. Kirkitadze, M.D. and Barlow, P.N. 2001. Structure and flexibility of the multidomain proteins that serve as regulators of complement activation. Immunol. Rev. 180: 146-161.
21. Kirkitadze, M.D., Dryden, D.T.F., Kelly, S.M., Price, N.C., Wang, X., Krych, M., Atkinson, J.P., and Barlow, P.N. 1999a. Co-operativity between modules within a C3b-binding site of complement receptor type 1. FEBS Lett. 459: 133-138.
22. Kirkitadze, M.D., Henderson, C., Price, N.C., Kelly, S.M., Mullin, N.P., Parkinson, J., Dryden, D.T.F., and Barlow, P.N. 1999b. Central modules of the Vaccinia virus complement control protein are not in extensive contact. Biochem. J. 343: 167-175.
23. Kirkitadze, M.D., Krych, M., Uhrin, D., Dryden, D.T.F., Cooper, A., Wang, X., Hauhart, R., Atkinson, J.P., and Barlow, P.N. 1999c. Independently melting modules and highly structured intermodular junctions within complement receptor type 1. Biochemistry 38: 7019-7031.
24. 1H 2D NMR spectra by interactive graphics. J. Magn. Reson. 24: 627-633.
25. -. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
26. Krych, M., Hourcade, D., and Atkinson, J.P. 1991. Sites within the complement C3b/C4b receptor important for the specificity of ligand binding. Proc. Natl. Acad. Sci. 88: 4353-4357.
27. Krych, M., Clemenza, L., Howdeshell, D., Hauhart, R., Hourcade, D., and Atkinson, J.P. 1994. Analysis of the functional domains of complement receptor-type-1 (C3b/C4b receptor, CD35) by substitution mutagenesis receptor-type-1 (C3b/C4b receptor, CD35) by substitution mutagenesis. J. Biol. Chem. 269: 13273-13278.
28. Krych, M., Hauhart, R., and Atkinson, J.P. 1998. Structure-function analysis of the active sites of complement receptor type 1. J. Biol. Chem. 273: 8623-8629.
29. Krych-Goldberg, M. and Atkinson, J.P. 2001. Structure-function relationships of complement receptor type 1. Immunol. Rev. 180: 112-122.
30. Krych-Goldberg, M., Moulds, J.M., and Atkinson, J.P. 2002. Human complement receptor type 1 (CR1) binds to a major malarial adhesin. Trends Mol. Med. 8: 531-537.
31. Kuboniwa, H., Grzesiek, S., Delaglio, F., and Bax, A. 1994. Measurement of HNHA J-couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4: 871-878.
32. Lipari, G. and Szabo, A. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules, 1: Theory and range of validity. J. Am. Chem. Soc. 104: 4546-4559.
33. Liszewski, M.K., Post, T.W., and Atkinson, J.P. 1991. Membrane cofactor protein (MCP or CD46): Newest member of the regulators of complement activation gene cluster. Annu. Rev. Immunol. 9: 431-455.
34. Liszewski, M.K., Leung, M.K., and Atkinson, J.P. 1998. Membrane cofactor protein: Importance of N- and O-glycosylation for complement regulatory function. J. Immunol. 161: 3711-3718.
35. Liszewski, M.K., Leung, M., Cui, W., Subramanian, V.B., Parkinson, J., Barlow, P.N., Manchester, M., and Atkinson, J.P. 2000. Dissecting sites important for complement regulatory activity in membrane cofactor protein (MCP; CD46). J. Biol. Chem. 275: 37692-37701.
36. Maisner, A., Alvarez, J., Liszewski, M.K., Atkinson, D.J., Atkinson, J.P., and Herrler, G. 1996. The N-glycan of the SCR 2 region is essential for membrane cofactor protein (CD46) to function as a measles virus receptor. J. Virol. 70: 4973-4977.
37. Manchester, M., Gairin, J.E., Patterson, J.B., Alvarez, J., Liszewski, M.K., Eto, D.S., Atkinson, J.P., and Oldstone, M.B. 1997. Measles virus recognizes its receptor, CD46, via two distinct binding domains within SCR1-2. Virology 233: 174-184.
38. Mandel, A.M., Akke, M., and Palmer, A.G. 1995. Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme. J. Mol. Biol. 246: 144-163.
39. McKercher, S.R., Lombardo, C.R., Bobkov, A., Jia, X., and Assa-Munt, N. 2003. Identification of a PU. 1-IRF4 protein interaction surface predicted by chemical exchange line broadening. Proc. Natl. Acad. Sci. 100: 511-516.
40. Medof, M.E., Lublin, D.M., Holers, V.M., Ayers, D.J., Getty, R.R., Leykam, J.F., Atkinson, J.P., and Tykocinski, M.L. 1987. Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement. Proc. Natl. Acad. Sci. 84: 2007-2011.
41. Murthy, K., Smith, S.A., Ganesh, V.K., Judge, K.W., Mullin, N., Barlow, P.N., Ogata, C.M., and Kotwal, G. 2001. Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans. Cell 104: 301-311.
42. Pangburn, M.K. 2000. Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement. Immunopharmacology 49: 149-157.
43. Reid, K.B.M. and Day, A.J. 1988. Structure-function relationships of the complement components. Immunol. Today 10: 177-180.
44. Smith, B.O., Mallin, R.L., Krych-Goldberg, M., Wang, X., Hauhart, R.E., Bromek, K., Uhrin, D., Atkinson, J.P., and Barlow, P.N. 2002. Structure of the C3b-binding site of CR1 (CD35), the immune adherence receptor. Cell 108: 769-780.
45. Uhrinova, S., Lin, F., Ball, G., Bromek, K., Uhrin, D., Medof, M.E., and Barlow, P.N. 2003. Solution structure of a functionally active fragment of decay-accelerating factor. Proc. Natl. Acad. Sci. 100: 4718-4723.
46. Walport, M.J. 2001. Complement: Second of two parts. N. Engl. J. Med. 344: 1140-1144.
47. Wand, A.J. 2001. Dynamic activation of protein function: A view emerging from NMR spectroscopy. Nat. Struct. Biol. 8: 926-931.
48. Weisman, H.F., Bartow, T., Leppo, M.K., Marsh Jr., H., Carson, G.R., Concino, M.F., Boyle, M.P., Roux, K.H., Weisfeldt, M.L., and Fearon, D.T. 1990. Soluble human complement receptor type 1: In vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis. Science 249: 146-151.
49. Wikstrom, A., Berglund, H., Hambraeus, C., van den Berg, S., and Hard, T. 1999. Conformational dynamics and molecular recognition: Backbone dynamics of the estrogen receptor DNA-binding domain. J. Mol. Biol. 289: 963-979.
50. Williams, P., Chaudhry, Y., Goodfellow, I.G., Billington, J., Powell, R., Spiller, O.B., Evans, D.J., and Lea, S. 2003. Mapping CD55 function: The structure of two pathogen-binding domains at 1.7 Ångstrom. J. Biol. Chem. 278: 10691-10696.