Human thrombospondin's (TSP-1) C-terminal domain opens to interact with the CD-47 receptor: A molecular modeling study

Archives of Biochemistry and Biophysics

Volumn 478, Issue 1, 2008, Pages 103-109

  Floquet, Nicolas ^a,b   Dedieu, Stéphane ^b   Martiny, Laurent ^b   Dauchez, Manuel ^b   Perahia, David ^c  

^a UNIVERSITÉ DE MONTPELLIER   (France)

^b CNRS   (France)

^c INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

Author keywords

CD 47; Docking; Hydrophobic cleft; Normal modes; Opening motion; Protein protein interactions; Thrombospondin; TSP 1

Indexed keywords

ARGININE; CD47 ANTIGEN; LYSINE; MEMBRANE RECEPTOR; METHIONINE; PHENYLALANINE; SOLVENT; THROMBOSPONDIN 1; TRYPTOPHAN; VALINE;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENERGY; HYDROPHOBICITY; MOLECULAR DOCKING; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

ANTIGENS, CD47; COMPUTER SIMULATION; HUMANS; KINETICS; MEMBRANE GLYCOPROTEINS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; THROMBOSPONDIN 1;

EID: 51249115387     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.07.015     Document Type: Article

References (36)

1. Elzie C.A., and Murphy-Ullrich J.E. Int. J. Biochem. Cell. Biol. 36 (2004) 1090-1101
2. Sid B., Sartelet H., Bellon G., El Btaouri H., Rath G., Delorme N., Haye B., and Martiny L. Crit. Rev. Oncol. Hematol. 49 (2004) 245-258
3. Rath G.M., Schneider C., Dedieu S., Rothhut B., Soula-Rothhut M., Ghoneim C., Sid B., Morjani H., El Btaouri H., and Martiny L. Biochim. Biophys. Acta 1763 (2006) 1125-1134
4. Saumet A., Slimane M.B., Lanotte M., Lawler J., and Dubernard V. Blood 106 (2005) 658-667
5. Grimbert P., Bouguermouh S., Baba N., Nakajima T., Allakhverdi Z., Braun D., Saito H., Rubio M., Delespesse G., and Sarfati M. J. Immunol. 177 (2006) 3534-3541
6. Lamy L., Foussat A., Brown E.J., Bornstein P., Ticchioni M., and Bernard A. J. Immunol. 178 (2007) 5930-5939
7. Kaczorowski D.J., and Billiar T.R. Circ. Res. 100 (2007) 602-603
8. Trumel C., Plantavid M., Levy-Toledano S., Ragab A., Caen J.P., Aguado E., Malissen B., and Payrastre B. J. Thromb. Haemost. 1 (2003) 320-329
9. Gao A.G., Lindberg F.P., Finn M.B., Blystone S.D., Brown E.J., and Frazier W.A. J. Biol. Chem. 271 (1996) 21-24
10. Kosfeld M.D., and Frazier W.A. J. Biol. Chem. 268 (1993) 8808-8814
11. Kvansakul M., Adams J.C., and Hohenester E. EMBO J. 23 (2004) 1223-1233
12. Q. Cui, I. Bahar, Normal Modes Analysis: Theory and Applications to Biological and Chemical Systems, Chapman & Hall/CRC, 2006.
13. Taly A., Delarue M., Grutter T., Nilges M., Le Novere N., Corringer P.J., and Changeux J.P. Biophysics J88 (2005) 3954-3965
14. Delarue M., and Dumas P. Proc. Natl. Acad. Sci. USA 101 (2004) 6957-6962
15. Lindahl E., and Delarue M. Nucleic Acids Res. 33 (2005) 4496-4506
16. May A., and Zacharias M. Proteins 70 (2008) 794-809
17. Floquet N., Marechal J.D., Badet-Denisot M.A., Robert C.H., Dauchez M., and Perahia D. FEBS Lett. 580 (2006) 5130-5136
18. Phillips J.C., Braun R., Wang W., Gumbart J., Tajkhorshid E., Villa E., Chipot C., Skeel R.D., Kale L., and Schulten K. J. Comput. Chem. 26 (2005) 1781-1802
19. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., and Karplus M. J. Comput. Chem. 4 (1983) 187-217
20. MacKerell A.D., Bashford D., Bellott M., Dunbrack R.L., Evanseck J.D., Field M.J., Fischer S., Gao J., Guo H., Ha S., Joseph-McCarthy D., Kuchnir L., Kuczera K., Lau F.T.K., Mattos C., Michnick S., Ngo T., Nguyen D.T., Prodhom B., Reiher W.E., Roux B., Schlenkrich M., Smith J.C., Stote R., Straub J., Watanabe M., Wiorkiewicz-Kuczera J., Yin D., and Karplus M. J. Phys. Chem. B3586-B3616 102 (1998) 3586-3616
21. Darden T.A., York D.M., and Pedersen L.G. J. Chem. Phys. 98 (1993) 10089-10092
22. Perahia D., and Mouawad L. Comput. Chem. 19 (1995) 241-246
23. Guilbert C., Perahia D., and Mouawad L. Comput. Phys. Commun. 91 (1995) 263-273
24. Humphrey W., Dalke A., and Schulten K. J. Mol. Graph. 14 (1996) 33-38
25. Andreeva A., Howorth D., Brenner S.E., Hubbard T.J., Chothia C., and Murzin A.G. Nucleic Acids Res. 32 (2004) D226-D229
26. Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. J. Mol. Biol. 247 (1995) 536-540
27. Shi J., Blundell T.L., and Mizuguchi K. J. Mol. Biol. 310 (2001) 243-257
28. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. Nucleic Acids Res. 25 (1997) 4876-4882
29. Sali A., and Blundell T.L. J. Mol. Biol. 234 (1993) 779-815
30. Russell R.B., and Barton G.J. Proteins 14 (1992) 309-323
31. Suhre K., and Sanejouand Y.H. Nucleic Acids Res. 32 (2004) 610-614
32. Lawler J., Chao F.C., and Cohen C.M. J. Biol. Chem. 257 (1982) 12257-12265
33. Lawler J., Derick L.H., Connolly J.E., Chen J.H., and Chao F.C. J. Biol. Chem. 260 (1985) 3762-3772
34. Hayward S., and Berendsen H.J. Proteins 30 (1998) 144-154
35. Hayward S., Kitao A., and Berendsen H.J. Proteins 27 (1997) 425-437
36. Sasaki T., Knyazev P.G., Clout N.J., Cheburkin Y., Gohring W., Ullrich A., Timpl R., and Hohenester E. EMBO J. 25 (2006) 80-87