메뉴 건너뛰기




Volumn 46, Issue 19, 2007, Pages 5687-5696

Mutagenesis of p38α MAP kinase establishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-OUT state

Author keywords

[No Author keywords available]

Indexed keywords

MAP KINASE STRUCTURE; X-RAY CRYSTAL STRUCTURES;

EID: 34248569419     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0622221     Document Type: Article
Times cited : (35)

References (37)
  • 2
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han, J., Lee, J. D., Bibbs, L., and Ulevitch, R. J. (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells, Science 265, 808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 3
    • 0032850020 scopus 로고    scopus 로고
    • p38α MAPK signaling cascades in inflammatory disease
    • Herlaar, E., and Brown, Z. (1999) p38α MAPK signaling cascades in inflammatory disease, Mol. Med. Today 5, 439-447.
    • (1999) Mol. Med. Today , vol.5 , pp. 439-447
    • Herlaar, E.1    Brown, Z.2
  • 5
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L. N., Noble, M. E., and Owen, D. J. (1996) Active and inactive protein kinases: structural basis for regulation, Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 6
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • Nolen, B., Taylor, S., and Ghosh, G. (2004) Regulation of protein kinases: controlling activity through activation segment conformation, Mol. Cell 15, 661-675.
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 7
    • 23644452511 scopus 로고    scopus 로고
    • Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component?
    • Kannan, N., and Neuwald, A. F. (2005) Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component?, J. Mol. Biol. 351, 956-972.
    • (2005) J. Mol. Biol , vol.351 , pp. 956-972
    • Kannan, N.1    Neuwald, A.F.2
  • 11
    • 4944261336 scopus 로고    scopus 로고
    • Structural insights into the conformational selectivity of STI-571 and related kinase inhibitors
    • Mol, C. D., Fabbro, D., and Hosfield, D. J. (2004) Structural insights into the conformational selectivity of STI-571 and related kinase inhibitors, Curr. Opin. Drug Discovery Dev. 7, 639-648.
    • (2004) Curr. Opin. Drug Discovery Dev , vol.7 , pp. 639-648
    • Mol, C.D.1    Fabbro, D.2    Hosfield, D.J.3
  • 12
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • Knight, Z. A., and Shokat, K. M. (2005) Features of selective kinase inhibitors, Chem. Biol. 12, 621-637.
    • (2005) Chem. Biol , vol.12 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2
  • 13
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu, Y., and Gray, N. S. (2006) Rational design of inhibitors that bind to inactive kinase conformations, Nat. Chem. Biol. 2, 358-364.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 14
    • 33745880692 scopus 로고    scopus 로고
    • Computational sampling of a cryptic drug binding site in a protein receptor: Explicit solvent molecular dynamics and inhibitor docking to p38 MAP kinase
    • Frembgen-Kesner, T., and Elcock, A. H. (2006) Computational sampling of a cryptic drug binding site in a protein receptor: explicit solvent molecular dynamics and inhibitor docking to p38 MAP kinase, J. Mol. Biol. 359, 202-214.
    • (2006) J. Mol. Biol , vol.359 , pp. 202-214
    • Frembgen-Kesner, T.1    Elcock, A.H.2
  • 18
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor
    • Matulis, D., Kranz, J. K., Salemme, F. R., and Todd, M. J. (2005) Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor, Biochemistry 44, 5258-5266.
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Macromol. Crystallogr. A 276, 307-326.
    • (1997) Macromol. Crystallogr. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor, S. S., and Radzio-Andzelm, E. (1994) Three protein kinase structures define a common motif, Structure 2, 345-355.
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 25
    • 1642270826 scopus 로고    scopus 로고
    • Recent kinase and kinase inhibitor x-ray structures: Mechanisms of inhibition and selectivity insights
    • Cherry, M., and Williams, D. H. (2004) Recent kinase and kinase inhibitor x-ray structures: mechanisms of inhibition and selectivity insights, Curr. Med. Chem. 11, 663-673.
    • (2004) Curr. Med. Chem , vol.11 , pp. 663-673
    • Cherry, M.1    Williams, D.H.2
  • 26
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M., and Kuriyan, J. (2002) The conformational plasticity of protein kinases, Cell 109, 275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 29
    • 21244476768 scopus 로고    scopus 로고
    • BIRB 796 inhibits all p38 MAPK isoforms in vitro and in vivo
    • Kuma, Y., Sabio, G., Bain, J., Shapiro, N., Márquez, R., and Cuenda, A. (2005) BIRB 796 inhibits all p38 MAPK isoforms in vitro and in vivo, J. Biol. Chem. 280, 19472-19479.
    • (2005) J. Biol. Chem , vol.280 , pp. 19472-19479
    • Kuma, Y.1    Sabio, G.2    Bain, J.3    Shapiro, N.4    Márquez, R.5    Cuenda, A.6
  • 30
    • 26444592983 scopus 로고    scopus 로고
    • Crystal Structure of Mnk2 kinase domain reveal an inhibitory conformation and a Zinc binding site
    • Jauch, R., Jäkel, S., Netter, C., Schreiter, K., Aicher, B., Jäckle, H., and Wahl, M. C. (2005) Crystal Structure of Mnk2 kinase domain reveal an inhibitory conformation and a Zinc binding site, Structure 13, 1559-1568.
    • (2005) Structure , vol.13 , pp. 1559-1568
    • Jauch, R.1    Jäkel, S.2    Netter, C.3    Schreiter, K.4    Aicher, B.5    Jäckle, H.6    Wahl, M.C.7
  • 31
    • 0033567706 scopus 로고    scopus 로고
    • The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation
    • Bellon, S., Fitzgibbon, M. J., Fox, T., Hsiao, H. M., and Wilson, K. P. (1999) The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation, Structure 7, 1057-1065.
    • (1999) Structure , vol.7 , pp. 1057-1065
    • Bellon, S.1    Fitzgibbon, M.J.2    Fox, T.3    Hsiao, H.M.4    Wilson, K.P.5
  • 32
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev, A. P., Haste, N. M., Taylor, S. S., and Ten Eyck, L. F. (2006) Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism, Proc. Nat. Acad. Sci. U.S.A. 103, 17783-17788.
    • (2006) Proc. Nat. Acad. Sci. U.S.A , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Ten Eyck, L.F.4
  • 33
    • 26244443673 scopus 로고    scopus 로고
    • Hydrogen exchange solvent protection by an ATP analogue reveals conformational changes in ERK2 upon activation
    • Lee, T., Hoofnagle, A. N., Resing, K. A., and Ahn, N. G. (2005) Hydrogen exchange solvent protection by an ATP analogue reveals conformational changes in ERK2 upon activation, J. Mol. Biol. 353, 600-612.
    • (2005) J. Mol. Biol , vol.353 , pp. 600-612
    • Lee, T.1    Hoofnagle, A.N.2    Resing, K.A.3    Ahn, N.G.4
  • 35
    • 0032524350 scopus 로고    scopus 로고
    • Autoregulatory mechanisms in protein-tyrosine kinases
    • Hubbard, S. R., Mohammadi, M., and Schlessinger, J. (1998) Autoregulatory mechanisms in protein-tyrosine kinases, J. Biol. Chem. 273, 11987-11990.
    • (1998) J. Biol. Chem , vol.273 , pp. 11987-11990
    • Hubbard, S.R.1    Mohammadi, M.2    Schlessinger, J.3
  • 36
    • 9944247211 scopus 로고    scopus 로고
    • Novel protein kinases and molecular mechanisms of autoinhibition
    • Cheetham, G. M. T. (2004) Novel protein kinases and molecular mechanisms of autoinhibition, Curr. Opin. Struct. Biol. 14, 700-705.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 700-705
    • Cheetham, G.M.T.1
  • 37
    • 33745253917 scopus 로고    scopus 로고
    • A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Gay, L. M., Ng, H.-L., and Alber, T. (2006) A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis, J. Mol. Biol. 360, 409-420.
    • (2006) J. Mol. Biol , vol.360 , pp. 409-420
    • Gay, L.M.1    Ng, H.-L.2    Alber, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.