Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4

Journal of Molecular Biology

Volumn 401, Issue 3, 2010, Pages 389-402

  Filippakopoulos, Panagis ^a   Low, Andrew ^b   Sharpe, Timothy D ^a   Uppenberg, Jonas ^a   Yao, Shenggen ^b   Kuang, Zhihe ^b   Savitsky, Pavel ^a   Lewis, Rowena S ^b   Nicholson, Sandra E ^b   Norton, Raymond S ^b   Bullock, Alex N ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

ITC; NMR; Protein structure; Protein peptide interaction; X ray crystallography

Indexed keywords

ASPARTIC ACID; BINDING PROTEIN; HELICASE; HOMEODOMAIN PROTEIN; PROTEIN PAR 4; PROTEIN SPSB1; PROTEIN SPSB2; PROTEIN SPSB4; RNA HELICASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; DDX4 PROTEIN, HUMAN; DDX4 PROTEIN, MOUSE; DEAD BOX PROTEIN; PROTEASE-ACTIVATED RECEPTOR 4; PROTEIN BINDING; SSB-1 PROTEIN, MOUSE; SUPPRESSOR OF CYTOKINE SIGNALING; THROMBIN RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; DROSOPHILA; ENZYME SUBSTRATE; GENE MUTATION; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY; ANIMAL; CHEMISTRY; CONSENSUS SEQUENCE; HUMAN; METABOLISM; MOUSE; PROTEIN CONFORMATION;

MAMMALIA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CONSENSUS SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DEAD-BOX RNA HELICASES; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICE; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, THROMBIN; SUPPRESSOR OF CYTOKINE SIGNALING PROTEINS;

EID: 77955269719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.017     Document Type: Article

References (36)

1. 2+-release channels). Trends Biochem. Sci. 1997, 22:193-194.
2. Hilton D.J., Richardson R.T., Alexander W.S., Viney E.M., Willson T.A., Sprigg N.S., et al. Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl Acad. Sci. USA 1998, 95:114-119.
3. Kile B.T., Schulman B.A., Alexander W.S., Nicola N.A., Martin H.M., Hilton D.J. The SOCS box: a tale of destruction and degradation. Trends Biochem. Sci. 2002, 27:235-241.
4. Wang D., Li Z., Messing E.M., Wu G. The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response element pathway. J. Biol. Chem. 2005, 280:16393-16401.
5. Masters S.L., Yao S., Willson T.A., Zhang J.G., Palmer K.R., Smith B.J., et al. The SPRY domain of SSB-2 adopts a novel fold that presents conserved Par-4-binding residues. Nat. Struct. Mol. Biol. 2006, 13:77-84.
6. Sells S.F., Wood D.P., Joshi-Barve S.S., Muthukumar S., Jacob R.J., Crist S.A., et al. Commonality of the gene programs induced by effectors of apoptosis in androgen-dependent and -independent prostate cells. Cell Growth Differ. 1994, 5:457-466.
7. Garcia-Cao I., Duran A., Collado M., Carrascosa M.J., Martin-Caballero J., Flores J.M., et al. Tumour-suppression activity of the proapoptotic regulator Par4. EMBO Rep. 2005, 6:577-583.
8. Lafuente M.J., Martin P., Garcia-Cao I., Diaz-Meco M.T., Serrano M., Moscat J. Regulation of mature T lymphocyte proliferation and differentiation by Par-4. EMBO J. 2003, 22:4689-4698.
9. Styhler S., Nakamura A., Lasko P. VASA localization requires the SPRY-domain and SOCS-box containing protein, GUSTAVUS. Dev. Cell 2002, 3:865-876.
10. Woo J.S., Suh H.Y., Park S.Y., Oh B.H. Structural basis for protein recognition by B30.2/SPRY domains. Mol. Cell 2006, 24:967-976.
11. Letunic I., Copley R.R., Schmidt S., Ciccarelli F.D., Doerks T., Schultz J., et al. SMART 4.0: towards genomic data integration. Nucleic Acids Res. 2004, 32:D142-D144.
12. Henry J., Ribouchon M.T., Offer C., Pontarotti P. B30.2-like domain proteins: a growing family. Biochem. Biophys. Res. Commun. 1997, 235:162-165.
13. Rhodes D.A., de Bono B., Trowsdale J. Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence?. Immunology 2005, 116:411-417.
14. Kuang Z., Yao S., Xu Y., Lewis R.S., Low A., Masters S.L., et al. SPRY domain-containing SOCS box protein 2: crystal structure and residues critical for protein binding. J. Mol. Biol. 2009, 386:662-674.
15. Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H. Structural and functional insights into the B30.2/SPRY domain. EMBO J. 2006, 25:1353-1363.
16. Grutter C., Briand C., Capitani G., Mittl P.R., Papin S., Tschopp J., Grutter M.G. Structure of the PRYSPRY-domain: implications for autoinflammatory diseases. FEBS Lett. 2006, 580:99-106.
17. James L.C., Keeble A.H., Khan Z., Rhodes D.A., Trowsdale J. Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function. Proc. Natl Acad. Sci. USA 2007, 104:6200-6205.
18. Park E.Y., Kwon O.B., Jeong B.C., Yi J.S., Lee C.S., Ko Y.G., Song H.K. Crystal structure of PRY-SPRY domain of human TRIM72. Proteins 2010, 78:790-795.
19. He F., Saito K., Kobayashi N., Harada T., Watanabe S., Kigawa T., et al. Structural and functional characterization of the NHR1 domain of the Drosophila neuralized E3 ligase in the notch signaling pathway. J. Mol. Biol. 2009, 393:478-495.
20. Xing Y., Gosden R., Lasko P., Clarke H. Murine homologues of the Drosophila gustavus gene are expressed in ovarian granulosa cells. Reproduction 2006, 131:905-915.
21. 15N assignments of the 25 kDa SPRY domain-containing SOCS box protein 2 (SSB-2). J. Biomol. NMR 2005, 31:69-70.
22. Libich D.S., Schwalbe M., Kate S., Venugopal H., Claridge J.K., Edwards P.J., et al. Intrinsic disorder and coiled-coil formation in prostate apoptosis response factor 4. FEBS J. 2009, 276:3710-3728.
23. 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR 1995, 5:14-24.
24. 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 1995, 5:67-81.
25. Yao S., Liu M.S., Masters S.L., Zhang J.G., Babon J.J., Nicola N.A., et al. Dynamics of the SPRY domain-containing SOCS box protein 2: flexibility of key functional loops. Protein Sci. 2006, 15:2761-2772.
26. Masters S.L., Palmer K.R., Stevenson W.S., Metcalf D., Viney E.M., Sprigg N.S., et al. Genetic deletion of murine SPRY domain-containing SOCS box protein 2 (SSB-2) results in very mild thrombocytopenia. Mol. Cell. Biol. 2005, 25:5639-5647.
27. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 1995, 6:135-140.
28. Bartels C., Xia T.H., Billeter M., Güntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 1995, 6:1-10.
29. Leslie A.G.W., Powell H. MOSFLM 7.01 Edit 2007, MRC Laboratory of Molecular Biology, Cambridge, UK.
30. Evans P. SCALA-Scale Together Multiple Observations Of Reflections 3.3.0 Edit 2007, MRC Laboratory of Molecular Biology, Cambridge, UK.
31. Kabsch W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 1998, 21:67-71.
32. Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 1998, 21:916-924.
33. Sheldrick G.M. A short history of SHELX. Acta Crystallogr., Sect. A: Found. Crystallogr. 2008, 64:112-122.
34. McCoy A.J., Grosse-Kunstleve R.W., Storoni L.C., Read R.J. Likelihood-enhanced fast translation functions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2005, 61:458-464.
35. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60:2126-2132.
36. Painter J., Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006, 62:439-450.