Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment

Nature Structural Biology

Volumn 10, Issue 1, 2003, Pages 53-58

  Nishida, Noritaka ^a,b   Sumikawa, Hiromi ^b,c   Sakakura, Masayoshi ^a   Shimba, Nobuhisa ^b,c   Takahashi, Hideo ^d   Terasawa, Hiroaki ^a   Suzuki, Ei ichiro ^b,c   Shimada, Ichio ^a,d  

^a UNIVERSITY OF TOKYO   (Japan)

^b Japan Biological Information Research Center   (Japan)

^c AJINOMOTO CO INC   (Japan)

^d NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2 INTEGRIN; FIBRILLAR COLLAGEN; INTEGRIN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR A3;

ARTICLE; BINDING AFFINITY; BINDING SITE; HYDROPHILICITY; HYDROPHOBICITY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING;

BINDING SITES; COLLAGEN; DNA MUTATIONAL ANALYSIS; HUMANS; HYDROPHOBICITY; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; VON WILLEBRAND FACTOR;

EID: 0037222091     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb876     Document Type: Article

References (32)

1. Kadler, K.E., Holmes, D.F., Trotter, J.A. & Chapman, J.A. Collagen fibril formation. Biochem. J. 316, 1-11 (1996).
2. Juliano, R.L. & Haskill, S. Signal transduction from the extracellular matrix. J. Cell. Biol. 120, 577-585 (1993).
3. Foster, T.J. & Hook, M. Surface protein adhesins of Staphylococcus aureus. Trends Microbiol. 6, 484-488 (1998).
4. Colombatti, A. & Bonaldo, P. The superfamily of proteins with von Willebrand factor type A-like domains: One theme common to components of extracellular matrix, hemostasis, cellular adhesion, and defense mechanisms. Blood 77, 2305-2315 (1991).
5. Perkins, S.J. et al. The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. J. Mol. Biol. 238, 104-119 (1994).
6. Emsley, J., Knight, C.G., Farndale, R.W., Barnes, M.J. & Liddington, R.C. Structural basis of collagen recognition by integrin α2β1. Cell 101, 47-56 (2000).
7. Dickeson, S.K. & Santoro, S.A. Ligand recognition by the I domain-containing integrins. Cell. Mol. Life Sci. 54, 556-566 (1998).
8. Ruggeri, Z.M. von Willebrand factor. J. Clin. Invest. 99, 559-564 (1997).
9. Cruz, M.A., Yuan, H., Lee, J.R., Wise, R.J. & Handin, R.I. Interaction of the von Willebrand factor (vWF) with collagen. J. Biol. Chem. 270, 10822-10827 (1995).
10. Lankhof, H. et al. A3 domain is essential for interaction of von Willebrand factor with collagen type III. Thromb. Haemost. 75, 950-958 (1996).
11. Bienkowska, J., Cruz, M., Atiemo, A., Handin, R. & Liddington, R. The von Willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J. Biol. Chem. 272, 25162-25167 (1997).
12. Huizinga, E.G., van der Plas, R.M., Kroon, J., Sixma, J.J. & Gros, P. Crystal structure of the A3 domain of human von Willebrand factor: Implications for collagen binding. Structure 5, 1147-1156 (1997).
13. van der Plas, R.M. et al. Binding of von Willebrand factor to collagen type III: Role of specific amino acids in the collagen binding domain of vWF and effects of neighboring domains. Thromb. Haemost. 84, 1005-1011 (2000).
14. Romijn, R.A. et al. Identification of the collagen-binding site of the von Willebrand factor A3-domain. J. Biol. Chem. 276, 9985-9991 (2001).
15. Takahashi, H., Nakanishi, T., Kami, K., Arata, Y. & Shimada, I. A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 7, 220-223 (2000).
16. Nakanishi, T. et al. Determination of the interface of a large protein complex by transferred cross-saturation measurements. J. Mol. Biol. 318, 245-249 (2002).
17. Jayalakshmi, V. & Krishna, N.R. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. J. Magn. Reson. 155, 106-118 (2002).
18. 15N resonance assignments of the von Willebrand factor A3 domain. J. Biomol. NMR in the press (2002).
19. Ribba, A.S. et al. Ser968Thr mutation within the A3 domain of von Willebrand factor (vWF) in two related patients leads to a defective binding of VWF to collagen. Thromb. Haemost. 86, 848-854 (2001).
20. Verkleij, M.W. et al. Adhesive domains in the collagen III fragment α1 (III)C84 that support α2β1- and von Willebrand factor-mediated platelet adhesion under flow conditions. Thromb. Haemost. 82, 1137-1144 (1999).
21. Knight, C.G. et al. The collagen-binding A-domains of integrins α1β1 and α2β1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J. Biol. Chem. 275, 35-40 (2000).
22. Chen, J.M., Kung, C.E., Feairheller, S.H. & Brown, E.M. An energetic evaluation of a 'Smith' collagen microfibril model. J. Protein Chem. 10, 535-552 (1991).
23. Tuckwell, D. Evolution of von Willebrand factor A (VWA) domains. Biochem. Soc. Trans. 27, 835-840 (1999).
24. Clore, G.M. & Gronenborn, A.M. Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol. 239, 349-363 (1994).
25. Delaglio, F. et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
26. 1H 2D NMR spectra by interactive computer graphics. J. Mol. Biol. 184, 627-633 (1989).
27. Mori, S. et al. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delay using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. B 108, 94-98 (1995).
28. Kupce, E. & Wagner, G. Wideband homonuclear decoupling in protein spectra. J. Magn. Reson. B 109, 329-333 (1995).
29. Sasaki, T. et al. Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J. Biol. Chem. 272, 9237-9243 (1997).
30. Palma, P.N., Krippahl, L., Wampler, J.E. & Moura, J.J. BIGGER: A new (soft) docking algorithm for predicting protein interactions. Proteins 39, 372-384 (2000).
31. Kraulis, P. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 924-950 (1991).
32. Merritt, E.A. & Bacon, D.J. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).