Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate

Journal of Biological Chemistry

Volumn 274, Issue 15, 1999, Pages 10184-10189

  Meng, Qi ^a   Malinovskii, Vladimir ^a   Huang, Wen ^a   Hu, Yajing ^a   Chung, Linda ^b   Nagase, Hideaki ^b   Bode, Wolfram ^c   Maskos, Klaus ^c   Brew, Keith ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE; THREONINE; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

CELL LINE; CIRCULAR DICHROISM; COLLAGENASES; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; GELATINASES; KINETICS; MATRIX METALLOPROTEINASE 1; MATRIX METALLOPROTEINASE 2; MATRIX METALLOPROTEINASE 3; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TISSUE INHIBITOR OF METALLOPROTEINASE-1; UP-REGULATION;

EID: 0033538059     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.15.10184     Document Type: Article

References (36)

1. Woessner, J. F., Jr. (1994) Ann. N. Y. Acad. Sci. 732, 11-21
2. Nagase, H. (1996) in Zinc Metalloproteinases in Health and Disease (Hooper, N. M., ed) pp. 153-204, Taylor & Francis Ltd., London
3. Docherty, A. J. P., Lyons, A., Smith, B. J., Wright, E. M., Stephens, P. E., Harris, T. J. R., Murphy, G., and Reynolds, J. J. (1985) Nature 318, 66-69
4. Boone, T. C., Johnson, M. J., DeClerck, Y. A., and Langley, K. E. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 2800-2804
5. Pavloff, N., Staskus, P. W., Kishnani, N. S., and Hawkes, S. P. (1992) J. Biol. Chem. 267, 17321-17326
6. Silbiger, S. M., Jacobsen, V. L., Cupples, R. L., and Koski, R. A. (1994) Gene 141, 293-297
7. Greene, J., Wang, M., Liu, Y. E., Raymond, L. A., Rosen, C., and Shi, Y. E. (1996) J. Biol. Chem. 271, 30375-30380
8. Williamson, E. A., Marston, F. A. O., Angal, S., Koklitis, P., Panico, M., Morris, H. R., Carne, A. F., Smith, B. J., Harris, T. J. R., and Freedman, R. B. (1990) Biochem. J. 268, 267-274
9. Murphy, G., Houbrechts, A., Cockett, M. I., Williamson, R. A., O-Shea, M., and Docherty, A. J. P. (1991) Biochemistry 30, 8097-8102
10. O'Shea, M., Willenbrock, F., Williamson, R. A., Cockett, M. I., Freedman, R. B., Reynolds, J. J., Docherty, A. J. P., and Murphy, G. (1992) Biochemistry 31, 10146-10152
11. Huang, W., Suzuki, K., Nagase, H., Arumugam, S., Van Doren, S. R., and Brew, K. (1996) FEBS Lett. 384, 155-161
12. Murphy, G., and Willenbrock, F. (1995) Methods Enzymol. 248, 496-510
13. Bigg, H. F., Shi., Y. E., Liu, Y. E., Steffensen, B., and Overall, C. M. (1997) J. Biol. Chem. 272, 15496-15500
14. Will, H., Atkinson, S. J., Butler, G. S., Smith, B., and Murphy, G. (1996) J. Biol. Chem. 271, 17119-17123
15. Hayakawa, T., Yamashita, K., Tanzawa, K., Uchijima, E., and Iwata, K. (1992) FEBS Lett. 298, 29-31
16. Hayakawa, T., Yamashita, K., Ohuchi, E., and Shimagawa, A. (1994) J. Cell Sci. 107, 2373-2379
17. Anand-Apte, B., Pepper, M. S., Voest, E., Montesano, K., Olsen, B., Murphy, G., Apte, S., and Zetter, B. (1997) Invest. Opthalmol. Visual Sci. 38, 817-823
18. Gomis-Rüth, F-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K, Bourenkov, G. P., Bartunik, H., and Bode, W. (1997) Nature 389, 77-81
19. Fernandez-Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., and Maskos, K. (1998) EMBO J. 17, 5238-5248
20. Williamson, R. A., Martorell, G., Carr, M. D., Murphy, G., Docherty, A. J. P., Freedman, R. B., and Feeney, J. (1994) Biochemistry 33, 11745-11759
21. Muskett, F. W., Frenkiel, T. A., Feeney, J., Freedman, R. B., Carr, M. D., and Williamson, R. A. (1998) J. Biol. Chem. 273, 21736-21743
22. Murzin, A. G. (1993) EMBO J. 12, 861-867
23. Nagase, H., Suzuki, K., Cawston, T. E., and Brew, K. (1997) Biochem. J. 325, 163-167
24. Huang, W., Meng, Q., Suzuki, K., Nagase, H., and Brew, K. (1997) J. Biol. Chem. 272, 22086-22091
25. Sarkar, G., and Sommer, S. S. (1990) BioTechniques 8, 404-407
26. Nagase, H., Fields, C. G., and Fields, G. B. (1994) J. Biol. Chem. 269, 20952-20957
27. Knight, C. G., Willenbrock, F., and Murphy, G. (1992) FEBS Lett. 296, 263-266
28. Morrison, J. F., and Walsh, C. T. (1988) Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301
29. Nagase, H., and Fields, G. B. (1996) Biopolymers 40, 399-416
30. Roseman, M. A. (1988) J. Mol. Biol. 200, 513-522
31. Stams, T., Spurlino, J. C., Smith, D. L., Wahl, R. C., Ho, T. F., Qoronfleh, M. W., Banks, T. M., and Rubin, B. (1994) Nat. Struct. Biol. 1, 119-123
32. Jones, S., and Thornton, J. M. (1996) Proc. Natl. Acad. Sci. U. S. A. 93,13-20
33. Miller, S., Janin, J., Lesk, A. M., and Chothia, C. (1987) J. Mol. Biol. 196, 641-656
34. Clackson, T., and Wells, J. A. (1995) Science 267, 383-386
35. Wells, J. A. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 1-6
36. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950