메뉴 건너뛰기




Volumn 61, Issue 3, 2005, Pages 694-697

Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE; PROTEIN PHOSPHATASE VHY; UNCLASSIFIED DRUG;

EID: 27544484789     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20642     Document Type: Article
Times cited : (12)

References (20)
  • 1
    • 0036181649 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Structure and function, substrate specificity, and inhibitor development
    • Zhang ZY. Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development. Annu Rev Pharmacol Toxicol 2002;42:209-234.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 209-234
    • Zhang, Z.Y.1
  • 3
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A, Zhou MM. Structure and regulation of MAPK phosphatases. Cell Signal 2004;16:769-779.
    • (2004) Cell Signal , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 4
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • Yuvaniyama J, Denu JM, Dixon JE, Saper MA. Crystal structure of the dual specificity protein phosphatase VHR. Science 1996;272: 1328-1331.
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 5
    • 0035895980 scopus 로고    scopus 로고
    • Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation
    • Alonso A, Saxena M, Williams S, Mustelin T. Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation. J Biol Chem 2001;276:4766-4771.
    • (2001) J Biol Chem , vol.276 , pp. 4766-4771
    • Alonso, A.1    Saxena, M.2    Williams, S.3    Mustelin, T.4
  • 7
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie AG. Integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 1999;55:1696-1702.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1696-1702
    • Leslie, A.G.1
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 11
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 13
  • 14
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 15
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 1997;15:132-134.
    • (1997) J Mol Graph Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 16
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24: 946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 17
    • 0032910476 scopus 로고    scopus 로고
    • Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
    • Stewart AE, Dowd S, Keyse SM, McDonald NQ. Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation. Nat Struct Biol 1999;6:174-181.
    • (1999) Nat Struct Biol , vol.6 , pp. 174-181
    • Stewart, A.E.1    Dowd, S.2    Keyse, S.M.3    McDonald, N.Q.4
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 1999;99:323-334.
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 20
    • 0035265679 scopus 로고    scopus 로고
    • Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    • Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell 2001;7:615-626.
    • (2001) Mol Cell , vol.7 , pp. 615-626
    • Song, H.1    Hanlon, N.2    Brown, N.R.3    Noble, M.E.4    Johnson, L.N.5    Barford, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.