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Volumn 388, Issue 6643, 1997, Pages 693-697

Crystal structure of a small G protein in complex with the GTPase- activating protein rhoGAP

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE;

EID: 0030759770     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/41805     Document Type: Article
Times cited : (225)

References (29)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for divers cell functions
    • Bourne, H. R., Sanders, D. A. & McCormick, F. The GTPase superfamily: a conserved switch for divers cell functions. Nature 348, 125-132 (1990).
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A. & McCormick, F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127 (1991).
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 3
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21rho induces rapid changes in cell morphology
    • Paterson, H. F. et al. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 1001-1007
    • Paterson, H.F.1
  • 4
    • 0025078512 scopus 로고
    • The cellular functions of small GTP-binding proteins
    • Hall, A. The cellular functions of small GTP-binding proteins. Science 249, 635-640 (1990).
    • (1990) Science , vol.249 , pp. 635-640
    • Hall, A.1
  • 5
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J. & Hall, A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399 (1992).
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 6
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu, R.-G., Chen, J., Kim, D., McCormick, F. & Symns, M. An essential role for Rac in Ras transformation. Nature 374, 457-459 (1995).
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.-G.1    Chen, J.2    Kim, D.3    McCormick, F.4    Symns, M.5
  • 7
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • Ridley, A. J. Rho: theme and variations. Cum Biol 6, 1256-1264 (1996).
    • (1996) Cum Biol , vol.6 , pp. 1256-1264
    • Ridley, A.J.1
  • 8
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/ SAPK signaling pathway
    • Coso, O. A. et al. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/ SAPK signaling pathway. Cell 81, 1137-1146 (1995).
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1
  • 9
    • 0029070887 scopus 로고
    • Selective activation of the INK signaling cascade and c-Jun transcriptinal activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., Un, A., Claret, F.-X., Abo, A. & Karin, M. Selective activation of the INK signaling cascade and c-Jun transcriptinal activity by the small GTPases Rac and Cdc42Hs. Cell 81,1147-1157(1995).
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Un, A.2    Claret, F.-X.3    Abo, A.4    Karin, M.5
  • 10
    • 0027972582 scopus 로고
    • Characterization of rhoGAP
    • Lancaster, C. A. et al. Characterization of rhoGAP.J. Biol. Chem. 269, 1137-1142 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 1137-1142
    • Lancaster, C.A.1
  • 11
    • 0027984138 scopus 로고
    • GAPs for rho-rdated GTPases
    • Lamarche, N. & Hall, A. GAPs for rho-rdated GTPases, Trends Genet. 10, 436-440 (1994).
    • (1994) Trends Genet. , vol.10 , pp. 436-440
    • Lamarche, N.1    Hall, A.2
  • 12
    • 0027965652 scopus 로고
    • iα1 and the mechanism of GTP hydrolysis
    • iα1 and the mechanism of GTP hydrolysis. Science 265, 1405-1412 (1994).
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1
  • 13
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35A resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F. et al. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359 (1990).
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1
  • 14
    • 0025275582 scopus 로고
    • Time-resolved X-ray crystallographic study of the conformational change in HaRas p21 protein on GTP hydrolysis
    • Schlichting, I. et al. Time-resolved X-ray crystallographic study of the conformational change in HaRas p21 protein on GTP hydrolysis. Nature 345, 309-315 (1990).
    • (1990) Nature , vol.345 , pp. 309-315
    • Schlichting, I.1
  • 15
    • 0026596419 scopus 로고
    • X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis
    • Prive, G. G. et al. X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis. Proc. Natl Acad. Sci. USA 89, 3649-3653 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3649-3653
    • Prive, G.G.1
  • 16
    • 0031034136 scopus 로고    scopus 로고
    • The crystal structure of human racl, a member of the rho-family complexed with a GTP analogue
    • Hirshbergf M., Stockley, R. W., Dodson, G. & Webb, M. R. The crystal structure of human racl, a member of the rho-family complexed with a GTP analogue Nature Struct. Biol. 4, 147-152 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 147-152
    • Hirshbergf, M.1    Stockley, R.W.2    Dodson, G.3    Webb, M.R.4
  • 17
    • 0029829561 scopus 로고    scopus 로고
    • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
    • Scheffeel, K., Lautwein. A., Kabsch, W., Ahmadian, M. R. & Wittinghofer, A. Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature 384, 591-596 (1996).
    • (1996) Nature , vol.384 , pp. 591-596
    • Scheffeel, K.1    Lautwein, A.2    Kabsch, W.3    Ahmadian, M.R.4    Wittinghofer, A.5
  • 18
    • 18144437689 scopus 로고    scopus 로고
    • The structure of the GTPase-activating domain from pSOrhoGAP
    • Barren, T. et al. The structure of the GTPase-activating domain from pSOrhoGAP. Nature 385, 458-461 (1997).
    • (1997) Nature , vol.385 , pp. 458-461
    • Barren, T.1
  • 19
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTP-γS
    • Noel, J. P., Hamm, H. E, & Sigler, P. B. The 2.2 Å crystal structure of transducin-α complexed with GTP-γS. Nature 366, 654-663 (1993).
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 22
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn, M. V. et al. Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins. Science 247, 939-945 (1990).
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1
  • 23
    • 0027128699 scopus 로고
    • Studies on the structure and mechanism of H-ras p21
    • Goody, R. S. et al. Studies on the structure and mechanism of H-ras p21. Phil Trans. R. Sac. Lond. B 336, 3-11 (1992).
    • (1992) Phil Trans. R. Sac. Lond. B , vol.336 , pp. 3-11
    • Goody, R.S.1
  • 24
    • 0030036699 scopus 로고    scopus 로고
    • Formation of a transition-state analog of Ras GTPase reaction by Ras GDP, tetrafluoroaluminate, and GTPase-acuvating proteins
    • Mittal, R., Ahmadian, M. R., Goody, R. S. & Wttinghofer, A. Formation of a transition-state analog of Ras GTPase reaction by Ras GDP, tetrafluoroaluminate, and GTPase-acuvating proteins. Science 273, 115-117 (1996).
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, R.S.3    Wttinghofer, A.4
  • 25
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia colias fusions with glutathione S-transferase
    • Smith, D. B. & Johnson, K. S. Single-step purification of polypeptides expressed in Escherichia colias fusions with glutathione S-transferase, Gene 67, 31-40 (1988).
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 26
    • 1842412059 scopus 로고
    • eds Sawyer, L. Isaacs, N. & Bailey, S. (SERC Daresbury Laboratory, Warrington)
    • Otwinowski, Z. & Minor, W. Data Collection and Processing (eds Sawyer, L. Isaacs, N. & Bailey, S.) 556-562 (SERC Daresbury Laboratory, Warrington, 1993).
    • (1993) Data Collection and Processing , pp. 556-562
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0028103275 scopus 로고
    • CCP4 the CCP4 suite: Programs for protein crystallography
    • CCP4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zhou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. I Appl Crystallogr, 24, 946-950 (1991).
    • (1991) I Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.