Solution Structure of the Focal Adhesion Adaptor PINCH LIM1 Domain and Characterization of Its Interaction with the Integrin-linked Kinase Ankyrin Repeat Domain

Journal of Biological Chemistry

Volumn 276, Issue 7, 2001, Pages 4932-4939

  Velyvis, Algirdas ^a,b   Yang, Yanwu ^a   Wu, Chuanyue ^c   Qin, Jun ^a,b  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CHARACTERIZATION; ENZYMES; NUCLEAR MAGNETIC RESONANCE; PROTEINS; ZINC;

FOCAL ADHESION ADAPTORS;

BIOCHEMISTRY;

ADAPTOR PROTEIN; ANKYRIN; CYSTEINE; INTEGRIN; PHOSPHOTRANSFERASE; PINCH PROTEIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; DNA BINDING PROTEIN; INTEGRIN LINKED KINASE; INTEGRIN-LINKED KINASE; PROTEIN SERINE THREONINE KINASE;

ARTICLE; CELL ADHESION; CELL DIFFERENTIATION; CELL GROWTH; GEL FILTRATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; ANKYRIN REPEAT; DNA-BINDING PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SEQUENCE HOMOLOGY, AMINO ACID; ZINC FINGERS;

EID: 0035895898     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M007632200     Document Type: Article

References (37)

1. Freyd, G., Kim, S. K., and Horvitz, H. R. (1990) Nature 344, 876-879
2. Karlsson, O., Thor, S., Norberg, T., Ohlsson, H., and Edlund, T. (1990) Nature 344, 879-882
3. Michelsen, J. W., Sewell, A. K., Louis, H. A., Olsen, J. I., Davis, D. R., Winge, D. R., and Beckerle, M. C. (1994) J. Biol. Chem. 269, 11108-11113
4. Dawid, I. B., Toyama, R., and Taira, M. (1995) C. R. Acad. Paris Sci. III 318, 295-306
5. Dawid, I. B., Breen, J. J., and Toyama, R. (1998) Trends Genet. 14, 156-162
6. Perez-Alvarado, G. C., Miles, C., Michelsen, J. W., Louis, H. A., Winge, D. R., Beckerle, M. C., and Summers, M. F. (1994) Nat. Struct. Biol. 1, 388-398
7. Perez-Alvarado, G. C., Kosa, J. L., Louis, H. A., Beckerle, M. C., Winge, D. R., and Summers, M. F. (1996) J. Mol. Biol. 257, 153-174
8. Hammarstrom, A., Berndt, K. D., Sillard, R., Adermann, K., and Otting, G. (1996) Biochemistry 35, 12723-12732
9. Konrat, R., Weiskirchen, R., Krautler, B., and Bister, K. (1997) J. Biol. Chem. 272, 12001-12007
10. Kontaxis, G., Konrat, R., Krautler, B., Weiskirchen, R., and Bister, K. (1998) Biochemistry 37, 7127-7134
11. Yao, X., Perez-Alvarado, G. C., Louis, H. A., Pomies, P., Hatt, C., and Summers, M. F., and Beckerle, M. C. (1999) Biochemistry 38, 5701-5713
12. Kloiber, K., Weiskirchen, R., Krautler, B., Bister, K., and Konrat, R. (1999) J. Mol. Biol. 292, 893-908
13. Rearden, A. (1994) Biochem. Biophys. Res. Commun. 201, 1124-1131
14. Wu, C. (1999) J. Cell Sci. 112, 4485-4489
15. Dedhar, S. (2000) Curr. Opin. Cell Biol. 12, 250-256
16. Tu, Y., Li, F., Goicoechea, S., and Wu, C. (1999) Mol. Cell. Biol. 19, 2425-2434
17. Li, F., Zhang, Y., and Wu, C. (1999) J. Cell Sci. 112, 4589-4599
18. Hobert, O., Moerman, D. G., Clark, K. A., Beckerle, M. C., and Ruvkun, G. (1999) J. Cell Biol. 144, 45-57
19. Tu, Y., Li, F., and Wu, C. (1998) Mol. Biol. Cell 9, 3367-3382
20. Bax, A., and Grzesiek, S. (1993) Acc. Chem. Res. 26, 131-138
21. Clore, G. M., and Gronenborn, A. M. (1998) Trends Biotechnol. 16, 22-34
22. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293
23. Garrett, D. S., Powers, R., Gronenborn, A. M., and Clore, G. M. (1991) J. Magn. Reson. 95, 214-220
24. Wuthrich, K. (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons, Inc., New York
25. Pascal, S. M., Ratliff, N., and Kay, L. E. (1994) J. Magn. Reson. Ser. B 103, 197-201
26. Nilges, M., Clore, G. M., and Gronenborn, A. M. (1988) FEBS Lett. 229, 317-324
27. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., and Karplus, M. (1983) J. Comput. Chem. 4, 187-217
28. Diakun, G. P., Fairall, L., and Klug, A. (1986) Nature 324, 698-699
29. Lee, M. S., Gippert, G. P., Soman, K. V., Case, D. A., and Wright, P. E. (1989) Science 245, 635-637
30. Fletcher, C. M., Jones, D. N. M., Diamond, R., and Neuhaus, D. (1996) J. Biomol. NMR 8, 292-310
31. Brünger, A. T. (1993) X-PLOR Version 3.1 Manual, Yale University Press, New Haven, CT
32. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486
33. Nicholls, A., Sharp, K., and Honig, B. (1991) Proteins Struct. Funct. Genet. 11, 281-296
34. Koradi, R., Billeter, M., and Wuthrich, K. (1996) J. Mol. Graph. 14, 51-55
35. Spera, S., and Bax, A. (1991) J. Am. Chem. Soc. 113, 5490-5492
36. Marintchev, A., Mullen, M. A., Maciejewski, M. W., Pan, B., Gryk, M. R., and Mullen, G. P. (1999) Nat. Struct. Biol. 6, 884-893
37. Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Nucleic Acids Res. 25, 3389-3402