The structure of phosphorylated P38γ is monomeric and reveals a conserved activation-loop conformation

Structure

Volumn 7, Issue 9, 1999, Pages 1057-1065

  Bellon, Steve ^a   Fitzgibbon, Matthew J ^a   Fox, Ted ^a   Hsiao, Hsun Mei ^a   Wilson, Keith P ^a  

^a VERTEX PHARMACEUTICALS   (United States)

Author keywords

MAP kinase; P38 ; Phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE; ADENYLYLIMIDODIPHOSPHATE; MAGNESIUM; METHIONINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 10; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN TYROSINE KINASE; THREONINE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DIMERIZATION; METABOLISM; PHOSPHORYLATION; PROTEIN CONFORMATION;

ADENYLYL IMIDODIPHOSPHATE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME ACTIVATION; MAGNESIUM; METHIONINE; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 10; MITOGEN-ACTIVATED PROTEIN KINASES; MODELS, MOLECULAR; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN-TYROSINE KINASES; THREONINE;

EID: 0033567706     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80173-7     Document Type: Article

References (40)

1. 1. Davis, R.J. (1995). Transcriptional regulation by MAP kinases. Mol. Reprod. Dev. 42, 459-467.
2. 2. Cobb, M.H. & Goldsmith, E.J. (1995). How MAP kinases are regulated. J. Biol. Chem. 270, 14843-14846.
3. 3. Marshall, C.J. (1995). Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80, 179-185.
4. 4. Taylor, S.S. & Radzio-Andzlem, E. (1994). Three protein kinase structures define a common motif. Structure 2, 345-355.
5. 5. Kultz, D. (1998). Phylogenetic and functional classification of mitogen-and stress-activated protein kinases. J. Mol. Evol. 46, 571-588.
6. 6. Li, Z., Jiang, Y., Ulevitch, R.J. & Han, J. (1996). The primary structure of P38 γ: a new member of P38 group of MAP kinases. Biochem. Biophys. Res. Commun. 228, 334-340.
7. 7. Enslen, H., Raingeaud J. & Davis R.J. (1998). Selective activation of P38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6. J. Biol. Chem. 273, 1741-1748.
8. 8. Raingeaud, J., et al., & Davis, R.J. (1995). Pro-inflammatory cytokines and environmental stress cause P38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270, 7420-7426.
9. 9. Derijard, B., et al., & Davis, R.J. (1994). JNK1 : a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76, 1025-1037.
10. 10. Han, J., Lee, J.D., Bibbs, L. & Ulevitch, R.J. (1994). A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265, 808-811.
11. 11. Johnson, L.N., Noble, M.E.M. & Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
12. 12. Lee, J.C., et al., & Young, P.R. (1994). A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 372, 739-746.
13. 13. Young, P.R., et al., & Lee, J.C. (1997). Pyrimidyl imidazole inhibitors of P38 mitogen-activated protein kinase bind in the ATP site. J. Biol. Chem. 272, 12116-12121.
14. 14. Tong, L., et al., & Pargellis, C.A. (1997). A highly specific inhibitor of human P38 MAP kinase binds in the ATP pocket. Nat. Struct. Biol. 4, 311-316.
15. 15. Wilson, K.P., et al., & Su, M.S. (1997). The structural basis for the specificity of pyridinylimidazole inhibitors of P38 MAP kinase. Chem. Biol. 4, 423-431.
16. 16. Beyaert, R., et al., & Fiers, W. (1996). The P38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor. EMBO J. 15, 1914-1923.
17. 17. Crawley, J.B., Rawlinson, L., Lali, F.V., Page, T.H., Saklatvala, J. & Foxwell, B.M. (1997). T cell proliferation in response to interleukins 2 and 7 requires P38 MAP kinase activation. J. Biol. Chem. 272, 15023-15027.
18. 18. Fox, T., et al., & Wilson, K.P. (1998). A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of P38 MAP kinase. Protein Sci. 7, 2249-2255.
19. 19. Xie, X., et al., & Su, M.S. (1998). Crystal structure of JNK3: a kinase implicated in neuronal apoptosis. Structure 6, 983-991.
20. 20. Zhang, F., Strand, A., Robbins, D., Cobb, M.H. & Goldsmith, E.J. (1994). Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-711.
21. 21. Canagarajah, B.J., Khokhlatchev, A., Cobb, M.H. & Goldsmith, E.J. (1997). Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869.
22. 22. Zheng, J., et al., & Sowadski, J.M. (1993). 2.2 Å Refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr. D 49, 362-365.
23. 2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 12, 849-859.
24. 24. Narayana, N., Cox, S., Xuong, N.-h., Eyck, L.F.T. & Taylor, S.S. (1997). A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility. Structure 5, 921-935.
25. 25. Wilson, K.P., et al., & Su, M.S.-S. (1996). Crystal structure of P38 mitogen-activated protein kinase. J. Biol. Chem. 271, 27696-27700.
26. 26. Kumar, S., McLaughlin, M.M., McDonnell, P.C., Lee, J.C., Livi, G.P. & Young, P.R. (1995). Human mitogen-activated protein kinase CSBP1, but not CSBP2, complements a hog1 deletion in yeast. J. Biol. Chem. 270, 29043-29046.
27. 27. Robinson, M.J. & Cobb, M.H. (1997). Mitogen-activated protein kinase pathways. Curr. Opin. Cell Biol. 9, 180-186.
28. 28. Johnson, L.N. & O'Reilly, M. (1996). Control by phosphorylation. Curr. Opin. Struct. Biol. 6, 762-769.
29. 29. Yamaguchi, H. & Hendrickson, W.A. (1996). Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489.
30. 30. Johnson, L.N., Noble, M.E.M. & Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
31. 31. Russo, A.A., Jeffrey, P.D. & Pavletich, N.D. (1996). Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700.
32. 32. Khokhlatchev, A.V., et al., & Cobb, M.H. (1998) Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation. Cell 93, 605-615.
33. 33. Deiss, L.P., Feinstein, E., Berissi, H., Cohen, O. & Kimchi, A. (1995). Identification of a novel serine/threonine kinase and a novel 15 kD protein as potential mediators of the gamma interferon-induced cell death. Genes Dev. 9, 15-30.
34. 34. Okano, I., et al., & Mizuno, K. (1995). Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs. J. Biol. Chem. 270, 31321-31330.
35. 35. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of The CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S. eds), pp.56-62, SERC Daresbury laboratory, England.
36. 36. Minor, W. (1993). XDISPLAYF program. Purdue University.
37. 37. Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. (1994). Acta Crystallogr. D 50, 760-763.
38. 38. Sheldrick, G.M. (1990). Phase annealing in SHELX-90: Direct methods for larger structures. Acta Crystallogr. A 46, 467-473.
39. 39. Brünger, A.T., et al., & Warren, G.L. (1988). Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta. Crystallogr. D 54, 905-921.
40. 40. Carson, M. & Bugg, C.E. (1986). Algorithm for Ribbon Models of Proteins. J. Mol. Graphics 4, 121-122.