The Structure of Importin-β Bound to SREBP-2: Nuclear Import of a Transcription Factor

Science

Volumn 302, Issue 5650, 2003, Pages 1571-1575

  Lee, Soo Jae ^a   Sekimoto, Toshihiro ^a   Yamashita, Eiki ^a   Nagoshi, Emi ^a   Nakagawa, Atsushi ^a   Imamoto, Naoko ^a   Yoshimura, Masato ^a   Sakai, Hiroaki ^a   Chong, Khoon Tee ^a   Tsukihara, Tomitake ^a   Yoneda, Yoshihiro ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; CRYSTAL STRUCTURE; DIMERS; METABOLISM;

SURFACE STRUCTURES;

PROTEINS;

DIMER; KARYOPHERIN BETA; STEROL REGULATORY ELEMENT BINDING PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

BIOLOGY; PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; NUCLEAR IMPORT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; SURFACE PROPERTY;

ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BETA KARYOPHERINS; BINDING SITES; CELL NUCLEUS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA-BINDING PROTEINS; HELIX-LOOP-HELIX MOTIFS; HUMANS; HYDROPHOBICITY; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR LOCALIZATION SIGNALS; NUCLEAR PORE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RAN GTP-BINDING PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; TRANSCRIPTION FACTORS;

EID: 0345374584     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1088372     Document Type: Article

References (35)

1. M. S. Brown, J. L. Goldstein, Cell 89, 331 (1997).
2. J. Sakai et al., J. Biol. Chem. 272, 20213 (1997).
3. J. Sakai, A. Nohturfft, J. L. Goldstein, M. S. Brown J. Biol. Chem. 273, 5785 (1998).
4. A. H. Corbett, P. A. Silver, Microbiol. Mol. Biol. Rev. 61, 193 (1997).
5. D. Gorlich, U. Kutay, Annu. Rev. Cell Dev. Biol. 15, 607 (1999).
6. I. W. Mattaj, L. Englmeier, Annu. Rev. Biochem. 67, 265 (1998).
7. E. A. Nigg, Nature 386, 779 (1997).
8. S. Nakielny, G. Dreyfuss, Cell 99, 677 (1999).
9. K. Weis, Cell 112, 441 (2003).
10. S. Jakel, D. Gorlich, EMBO J. 17, 4491 (1998).
11. R. Truant, B. R. Cullen, Mol. Cell. Biol. 19, 1210 (1999).
12. D. Palmeri, M. H. Malim. Mol. Cell. Biol. 19, 1218 (1999).
13. C. K. Chan, S. Hubner, W. Hu, D. A. Jans, Gene Ther. 5, 1204 (1998).
14. M. H. Lam et al., J. Biol. Chem. 274, 7391 (1999).
15. J. D. Moore, J. Yang, R. Truant, S. Kornbluth, J. Cell. Biol. 144, 213 (1999).
16. A. Kurisaki, S. Kose, Y. Yoneda, C. H. Heldin, A. Moustakas, Mol. Biol. Cell 12, 1079 (2001).
17. E. Nagoshi, N. Imamoto, R. Sato, Y. Yoneda, Mol. Biol. Cell 10, 2221 (1999).
18. E. Nagoshi, Y. Yoneda, Mol. Cell. Biol. 21, 2779 (2001).
19. G. Cingolani, C. Petosa, K. Weis, C. W. Muller, Nature 399, 221 (1999).
20. G. Cingolani, J. Bednenko, M. T. Gillespie, L. Gerace, Mol. Cell 10, 1345 (2002).
21. I. R. Vetter, A. Arndt, U. Kutay, D. Gorlich, A. Wittinghofer, Cell 97, 635 (1999).
22. R. Bayliss, T. Littlewood, M. Stewart, Cell 102, 99 (2000).
23. S. J. Lee et al., J. Mol. Biol. 302, 251 (2000).
24. A. R. Ferre-D'Amare, G. C. Prendergast, E. B. Ziff, S. K. Burley, Nature 363, 38 (1993).
25. A. R. Ferre-D'Amare, P. Pognonec, R. G. Roeder, S. K. Burley, EMBO J. 13, 180 (1994).
26. A. Parraga, L. Bellsolell, A. R. Ferre-D'Amare, S. K. Burley, Structure 6, 661 (1998).
27. S. Hayward, H. J. C. Berendsen, Proteins 30, 144 (1996).
28. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, lie; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gin; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
29. X. Luo, M. Sawadogo, Mol. Cell. Biol. 16, 1367 (1996).
30. C. V. Dang, W. M. Lee, Mol. Cell. Biol. 8, 4048 (1988).
31. A. C. Saphire, S. J. Bark, L. Gerace, J. Biol. Chem. 273, 29764 (1998).
32. R. J. Read, Acta Crystallogr. A42, 140 (1986).
33. SHARP program for statistical heavy-atom refinement and phasing [E. L. Fortelle, G. Bricogne, Methods Enzymol. 276, 472 (1997)].
34. DM program for density modification [K. D. Cowtan, Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34 (1994)].
35. Supported by Grant-in-Aid for Scientific Research on Priority Areas (Y.Y.); Grant-in-Aid for Centers of Excellence (COE) Research from the Japanese Ministry of Education, Science, Sports, and Culture and the Human Frontier Science Program (Y.Y.); Grant-in-Aid for the New Energy and Industrial Technology Department Organization (NEDO), Japan (T.T.); and Grant-in-Aid for the 21st century COE Program from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT), Japan (T.T.).