The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site

Structure

Volumn 6, Issue 1, 1998, Pages 109-116

  Zhou, Hongjun ^a   Mazzulla, Marie J ^a   Kaufman, Joshua D ^b   Stahl, Stephen J ^b   Wingfield, Paul T ^b   Rubin, Jeffrey S ^c   Bottaro, Donald P ^c   Byrd, R Andrew ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Hairpin loop; Heparin binding; Hepatocyte growth factor (HGF); NMR

Indexed keywords

EID: 0032518610     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00012-4     Document Type: Article

References (43)

1. Miyazawa, K., et al., & Takahashi, K. (1989). Molecular cloning and sequence analysis of cDNA for human hepatocyte growth factor. Biochem. Biophys. Res. Commun. 163, 967-973.
2. Nakamura, T., et al., & Shimizu, S. (1989). Molecular cloning and expression of human hepatocyte growth factor. Nature 342, 440-443.
3. Matsumoto, K. & Nakamura, T. (1996). Emerging multipotent aspects of hepatocyte growth factor. J. Biochem. 119, 591-600.
4. Rosen, E.M., Nigam, S.K. & Goldberg, I.D. (1994). Scatter factor and the c-met receptor: a paradigm for mesenchymal/epithelial interaction. J. Cell Biol. 127, 1783-1787.
5. Zarnegar, R. & Michalopoulos, G.K. (1995). The many faces of hepatocyte growth factor: from hepatopoiesis to hematopoiesis. J. Cell Biol. 129, 1177-1180.
6. Rubin, J.S., Bottaro, D.P. & Aaronson, S.A. (1993). Hepatocyte growth factor/scatter factor and its receptor, the c-met proto-oncogene product. Biochem. Biophys. Acta 1155, 357-371.
7. Bottaro, D.P., et al., & Aaronson, S.A. (1991). Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product. Science 251, 802-804.
8. Naldini, L., Vigna, E., Narsimhan, R., Gaudino, G., Zarnegar, R., Michalopoulos, G.K. & Comoglio, P.M. (1991). Hepatocyte growth factor (HGF) stimulates the tyrosine kinase activity of the receptor encoded by the proto-oncogene c-MET. Oncogene 6, 501-504.
9. Higuchi, O., Mizuno, K., Vande Woude, G.F. & Nakamura, T. (1992). Expression of c-met proto-oncogene in COS cells induces the signal transducing high-affinity receptor for hepatocyte growth factor. FEBS Lett. 301, 282-286.
10. Cioce, V., et al., & Rubin, J.S. (1996). Hepatocyte growth factor (HGF)/NK1 is a naturally occurring HGF/scatter factor variant with partial agonist/antagonist activity. J. Biol. Chem. 271, 13110-13115.
11. Chan, A.M., Rubin, J.S., Bottaro, D.P., Hirschfield, D.W., Chedid, M. & Aaronson, S.A. (1991). Identification of a competitive HGF antagonist encoded by an alternative transcript. Science 254, 1382-1385.
12. Zioncheck, T.F., et al., & Stack, R.J. (1995). Sulfated oligosaccharides promote hepatocyte growth factor association and govern its mitogenic activity. J. Biol. Chem. 270, 16871-16878.
13. Schwall, R.H., et al., & Zioncheck, T.F. (1996). Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2. J. Cell Biol. 133, 709-718.
14. Sakata, H., et al., & Rubin, J.S. (1997). Heparin binding and oligomerization of hepatocyte growth factor/scatter factor isoforms. Heparan sulfate glycosaminoglycan requirement for Met binding and signaling. J. Biol. Chem. 272, 9457-9463.
15. Matsumoto, K., Takehara, T., Inoue, H., Hagiya, M., Shimizu, S. & Nakamura, T. (1991). Deletion of kringle domains or the N-terminal hairpin structure in hepatocyte growth factor results in marked decreases in related biological activities. Biochem. Biophys. Res. Commun. 181, 691-699.
16. Lokker, N.A., Presta, L.G. & Godowski, P.J. (1994). Mutational analysis and molecular modeling of the N-terminal kringle-containing domain of hepatocyte growth factor identifies amino acid side chains important for interaction with the c-Met receptor. Protein Eng. 7, 895-903.
17. Okigaki, M., Komada, M., Uehara, Y., Miyazawa, K. & Kitamura, N. (1992). Functional characterization of human hepatocyte growth factor mutants obtained by deletion of structural domains. Biochemistry 31, 9555-9561.
18. Mizuno K., et al., & Nakamura, T. (1994). Hairpin loop and second kringle domain are essential sites for heparin binding and biological activity of hepatocyte growth factor. J. Biol. Chem. 269, 1131-1136.
19. Lokker, N.A., et al., & Godowski, P.J. (1992). Structure-function analysis of hepatocyte growth factor: identification of variants that lack mitogenic activity yet retain high affinity receptor binding. EMBO J. 7, 2503-2510.
20. Donate, L.E., Gherardi, E., Srinivasan, N., Sowdhamini, R., Aparicio, S. & Blundell, T.L. (1994). Molecular evolution and domain structure of plasminogen-related growth factors (HGF/SF and HGF1/MSP). Protein Sci. 3, 2378-2394.
21. Stahl, S.J., et al., & Bottaro, D.P. (1997). Functional and biophysical characterization of recombinant human hepatocyte growth factor isoforms produced in Escherichia coli. Biochem. J. 326, 763-772.
22. 13C chemical-shift data. J. Biomol. NMR 4, 171-180.
23. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. Wiley, New York.
24. Reid, K.S.C., Lindley, P.F. & Thornton, J.M. (1985). Sulphur-aromatic interactions in proteins. FEBS Lett. 190, 209-213.
25. Jackson, R.L., Busch, S.J. & Cardin, A.D. (1991). Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 71, 481-539.
26. Faham, S., Hileman, R.E., Fromm, J.R., Linhardt, R.J. & Rees, D.C. (1996). Heparin structure and interactions with basic fibroblast growth factor. Science 271, 1116-1120.
27. Aoyama, H., et al., & Hayase, T. (1997). Isolation and conformational analysis of fragment peptide corresponding to the heparin-binding site of hepatocyte growth factor. Biochemistry 36, 10286-10291.
28. Lyon, M., Deakin, J.A., Mizuno, K., Nakamura, T. & Gallagher, J.T. (1994). Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants. J. Biol. Chem. 269, 11216-11223.
29. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
30. Muhandiram, D.R. & Kay, L.E. (1994). Gradient-enhanced tripleresonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B 103, 203-216.
31. 13C magnetization. J. Magn. Reson. B 101, 114-119.
32. 13C-labeled proteins via scalar couplings. J. Am. Chem. Soc. 115, 11054-11055.
33. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR 4, 845-858.
34. 13C-edited NOESY experiment J. Biomol. NMR 3, 463-470.
35. 13C-separated HMQC-NOESY-HMQC spectra using pulsed field gradients. J. Magn. Reson. B 101, 210-213.
36. Kuboniwa, H., Grzesiek, S., Delaglio, F. & Bax, A. (1994). Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4, 871-878.
37. Macura, S. & Ernst, R.R. (1980). Elucidation of cross relaxation in liquids by two-dimensional N.M.R. spectroscopy. Mol. Phys. 41, 95-117.
38. Altieri, A.S. & Byrd, R.A. (1995). Randomization approach to water suppression in multidimensional NMR using pulsed field gradients. J. Magn. Reson. B 107, 260-266.
39. Brünger, AT. (1992). X-PLOR 3.1: a System for X-ray Crystallography and NMR . Yale University Press, New Haven, CT.
40. Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988). Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Lett. 229, 317-324.
41. Koradi, R., Billeter, M. & Wüthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
42. Nicholls, A., Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
43. Sayle, R. & Milner-White, E.J. (1995). RasMol: biomolecular graphics for all. Trends Biochem. Sci. 20, 374.