Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family

Acta Crystallographica Section D: Biological Crystallography

Volumn 61, Issue 3, 2005, Pages 316-321

  Huang, Li Li ^a   Zhao, Xue Mei ^b   Huang, Chao Qun ^b   Yu, Long ^b   Xia, Zong Xiang ^a  

^a SHANGHAI INSTITUTE OF ORGANIC CHEMISTRY   (China)

^b FUDAN UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

CYCLOPHILIN; PRIMER DNA; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; CRYSTALLIZATION; HUMAN; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYCLOPHILINS; DNA PRIMERS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 24044434639     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444904033189     Document Type: Article

References (27)

1. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Gross-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, N., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
2. Etzkorn, F. A., Chang, Z., Stolz, L. A. & Walsh, C. T. (1994). Biochemistry, 33, 2380-2388.
3. Evans, S. V. (1993). J. Mol. Graph. 11, 134-138.
4. Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I. & Hill, C. P. (1996). Cell, 87, 1285-1294.
5. Goethel, S. F. & Marahiel, M. A. (1999). Cell. Mol. Life Sci. 55, 423-436.
6. Handschumacher, R. E., Harding, M. W., Rice, J., Drugge, R. & Speicher, D. W. (1984). Science, 226, 544-547.
7. Howard, B. R., Vajdos, F. F., Li, S., Sundquist, W. I. & Hill, C. P. (2003). Nature Struct. Biol. 10, 475-481.
8. Kallen, J., Spitzfaden, C., Zurini, M. G. M., Wider, G., Widmer, H., Wuthrich, K. & Walkinshaw, M. D. (1991). Nature (London), 353, 276-279.
9. Karmela, B. (1995). Acta Pharm. 45, 413-420.
10. Ke, H. (1992). J. Mol. Biol. 228, 539-550.
11. Ke, H., Mayrose, D. & Cao, W. (1993). Proc. Natl Acad. Sci. USA, 90, 3324-3328.
12. Ke, H., Zhao, Y., Luo, F., Weissman, I. & Friedman, J. (1993). Proc. Natl Acad. Sci. USA, 90, 11850-11854.
13. Ke, H., Zydowsky, L. D., Liu, J. & Walsh, C. T. (1991). Proc. Natl Acad. Sci. USA, 88, 9483-9487.
14. Luzzati, P. V. (1952). Acta Cryst. 5, 802-810.
15. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
16. Mikol, V., Kallen, J., Pflugl, G. & Walkinshaw, M. D. (1993). J. Mol. Biol. 234, 1119-1130.
17. Mikol, V., Kallen, J. & Walkinshaw, M. D. (1994). Proc. Natl Acad. Sci. USA, 91, 5183-5186.
18. Morris, A. L., MacArthur, M. W., Hutchinson, E. G. & Thornton, J. M. (1992). Proteins Struct. Funct. Genet. 12, 345-364.
19. Navaza, J. (1994). Acta Cryst. A50, 157-163.
20. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
21. Peterson, M. R., Hall, D. R., Berriman, M., Nunes, J. A., Leanard, G. A., Rairlamb, A. H. & Hunter, W. N. (2000). J. Mol. Biol. 298, 123-133.
22. Reidt, U., Wahl, M. C., Fasshauer, D., Horowitz, D. S., Luhrmann, R. & Ficner, R. (2003). J. Mol. Biol. 331, 45-56.
23. Roussel, A. & Cambillau, C. (1991). Silicon Graphics Partners Geometry Directory. Mountain View, CA, USA: Silicon Graphics.
24. Takahashi, N., Hayano, T. & Suzuki, M. (1989). Nature (London), 337, 473-478.
25. Zhao, Y., Chen, Y., Schutkowsky, M., Fischer, G. & Ke, H. (1997). Structure, 5, 139-146.
26. Zhao, Y. & Ke, H. (1996). Biochemistry, 35, 7362-7368.
27. Zhou, Z., Ying, K., Dai, J., Tang, R., Wang, W., Huang, Y., Zhao, W., Xie, Y. & Mao, Y. (2001). Cytogenet. Cell Genet. 92, 231-236.