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Volumn 16, Issue 18, 1997, Pages 5582-5591

Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS

Author keywords

Crystal structure; G proteins; GTP hydrolysis; Rap; Ras

Indexed keywords

CELL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROXYL GROUP; ONCOPROTEIN;

EID: 1842301722     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.18.5582     Document Type: Article
Times cited : (64)

References (55)
  • 1
    • 13344261980 scopus 로고    scopus 로고
    • Differential structural requirements for interaction of Ras protein with its distinct downstream effectors
    • Akasaka, K. et al. (1996) Differential structural requirements for interaction of Ras protein with its distinct downstream effectors. J. Biol. Chem., 271, 5353-5360.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5353-5360
    • Akasaka, K.1
  • 2
    • 0026047952 scopus 로고
    • Post-translational processing and subcellular localization of the ras-related rap2 protein
    • Béranger, F., Tavitian, A. and de Gunzburg, J. (1991) Post-translational processing and subcellular localization of the ras-related rap2 protein. Oncogene, 6, 1835-1842.
    • (1991) Oncogene , vol.6 , pp. 1835-1842
    • Béranger, F.1    Tavitian, A.2    De Gunzburg, J.3
  • 3
    • 0030023780 scopus 로고    scopus 로고
    • Combined effects of the signal sequence and the major chaperone proteins on the export of human cytokines in Escherichia coli
    • Bergès, H., Joseph-Liauzun, E. and Fayet, O. (1996) Combined effects of the signal sequence and the major chaperone proteins on the export of human cytokines in Escherichia coli. Appl. Environ. Microbiol., 62, 55-60.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 55-60
    • Bergès, H.1    Joseph-Liauzun, E.2    Fayet, O.3
  • 5
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M.S. and McCormick, F. (1993) Proteins regulating Ras and its relatives. Nature, 366, 643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 6
    • 0027458513 scopus 로고
    • Biology of the Rap proteins, members of the ras superfamily of GTP binding proteins
    • Bokoch, G.M. (1993) Biology of the Rap proteins, members of the ras superfamily of GTP binding proteins. Biochem. J., 289, 17-24.
    • (1993) Biochem. J. , vol.289 , pp. 17-24
    • Bokoch, G.M.1
  • 7
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A. and McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature, 349, 117-127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 8
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger, A.T., Karplus, M. and Petsko, G.A. (1989) Crystallographic refinement by simulated annealing: application to crambin. Acta Crystallogr. A, 45, 50-61.
    • (1989) Acta Crystallogr. A , vol.45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 9
    • 0027965652 scopus 로고
    • Structure of active conformations of Giα and the mechanism of GTP hydrolysis
    • Coleman, D.E., Berghuis, A.M., Lee, E., Linder, M.E., Gilman, A.G. and Sprang, S.R. (1994) Structure of active conformations of Giα and the mechanism of GTP hydrolysis. Science, 265, 1405-1412.
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 11
    • 0022471217 scopus 로고
    • Biological and biochemical properties of human rasH genes mutated at codon 61
    • Der, C., Finkel, T. and Cooper, G.M. (1986) Biological and biochemical properties of human rasH genes mutated at codon 61. Cell, 44, 167-176.
    • (1986) Cell , vol.44 , pp. 167-176
    • Der, C.1    Finkel, T.2    Cooper, G.M.3
  • 12
    • 0025346513 scopus 로고
    • Inhibition of GTPase activating protein stimulation of ras-p21 GTPase by the Krev-1 gene product
    • Frech, M., John, J., Pizon, V., Chardin, P., Tavitian, A., Clark, R., McCormick, F. and Wittinghofer, A. (1990) Inhibition of GTPase activating protein stimulation of ras-p21 GTPase by the Krev-1 gene product. Science, 249, 169-171.
    • (1990) Science , vol.249 , pp. 169-171
    • Frech, M.1    John, J.2    Pizon, V.3    Chardin, P.4    Tavitian, A.5    Clark, R.6    McCormick, F.7    Wittinghofer, A.8
  • 13
    • 0029665424 scopus 로고    scopus 로고
    • Conformational transitions in p21ras and its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP
    • Geyer, M., Schweins, T., Herrmann, C., Prisner, T., Wittinghofer, A. and Kalbitzer, H.R. (1996) Conformational transitions in p21ras and its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP. Biochemistry, 35, 10308-10320.
    • (1996) Biochemistry , vol.35 , pp. 10308-10320
    • Geyer, M.1    Schweins, T.2    Herrmann, C.3    Prisner, T.4    Wittinghofer, A.5    Kalbitzer, H.R.6
  • 14
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann, C., Spaargaren, M. and Wittinghofer, A. (1996) Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem., 271, 6794-6800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Spaargaren, M.2    Wittinghofer, A.3
  • 17
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the E. coli EF-Tu-EF-TS complex at 2.5 Å resolution
    • Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S. and Leberman, R. (1996) The structure of the E. coli EF-Tu-EF-TS complex at 2.5 Å resolution. Nature, 379, 511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 18
    • 0024600222 scopus 로고
    • A ras-related gene with transformation suppressor activity
    • Kitayama, H., Sugimoto, Y., Matsuzaki, T. Ikawa, Y. and Noda, M. (1989) A ras-related gene with transformation suppressor activity. Cell, 56, 77-84.
    • (1989) Cell , vol.56 , pp. 77-84
    • Kitayama, H.1    Sugimoto, Y.2    Matsuzaki, T.3    Ikawa, Y.4    Noda, M.5
  • 19
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: Variations on a theme
    • Kjeldgaard, M., Nyborg, J. and Clark, B.F.C. (1996) The GTP binding motif: variations on a theme. FASEB J., 10, 1347-1368.
    • (1996) FASEB J. , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 20
    • 0028204451 scopus 로고
    • Solution structure and dynamics of ras p21-GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis, P.J., Domaille, P.J., Campbell-Burk, S.L., Van Aken, T. and Laue, E.D. (1994) Solution structure and dynamics of ras p21-GDP determined by heteronuclear three-and four-dimensional NMR spectroscopy. Biochemistry, 33, 3515-3531.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 21
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright, D.G., Noel, J.P., Hamm, H.E. and Sigler, P.B. (1994) Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature, 369, 621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 23
    • 0024404145 scopus 로고
    • GTPase inhibiting mutations activate the a chain of Gs and stimulate adenylyl cyclase in human pituitary tumours
    • Landis, C.A., Masters, S.B., Spada, A., Pace, A.M., Bourne, H.R. and Vallar, L. (1989) GTPase inhibiting mutations activate the a chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature, 340, 692-696.
    • (1989) Nature , vol.340 , pp. 692-696
    • Landis, C.A.1    Masters, S.B.2    Spada, A.3    Pace, A.M.4    Bourne, H.R.5    Vallar, L.6
  • 24
    • 0025811611 scopus 로고
    • The product of the rap2 gene, member of the ras superfamily. Biochemical characterization and site directed mutagenesis
    • Lerosey, I., Chardin, P., de Gunzburg, J. and Tavitian, A. (1991) The product of the rap2 gene, member of the ras superfamily. Biochemical characterization and site directed mutagenesis. J. Biol. Chem., 266, 4315-4321.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4315-4321
    • Lerosey, I.1    Chardin, P.2    De Gunzburg, J.3    Tavitian, A.4
  • 25
    • 0031040253 scopus 로고    scopus 로고
    • Residues of the Rho family GTPases Rho and Cdc42 that specify sensitivity to Dbl-like guanine nucleotide exchange factors
    • Li, R. and Zheng, Y. (1997) Residues of the Rho family GTPases Rho and Cdc42 that specify sensitivity to Dbl-like guanine nucleotide exchange factors. J. Biol. Chem., 272, 4671-4679.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4671-4679
    • Li, R.1    Zheng, Y.2
  • 26
    • 0031024585 scopus 로고    scopus 로고
    • An intact Raf zinc finger is required for optimal binding to processed Ras and for Ras-dependent Raf activation in situ
    • Luo, Z., Dlaz, B., Marshall, M.S. and Avruch, J. (1997) An intact Raf zinc finger is required for optimal binding to processed Ras and for Ras-dependent Raf activation in situ. Mol. Cell. Biol., 17, 46-53.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 46-53
    • Luo, Z.1    Dlaz, B.2    Marshall, M.S.3    Avruch, J.4
  • 27
    • 0029781354 scopus 로고    scopus 로고
    • Ras-catalyzed hydrolysis of GTP: A new perspective from model studies
    • Maegley, K.A., Admiraal, S.J. and Herschlag, D. (1996) Ras-catalyzed hydrolysis of GTP: a new perspective from model studies. Proc. Natl Acad. Sci. USA, 93, 8160-8166.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8160-8166
    • Maegley, K.A.1    Admiraal, S.J.2    Herschlag, D.3
  • 28
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive torms of protooncogenic ras proteins
    • Milburn, M.V., Tong, L., DeVos, A.M., Brünger, A., Yamizumi, Z., Nishimura, S. and Kim, S.-H. (1990) Molecular switch for signal transduction: structural differences between active and inactive torms of protooncogenic ras proteins. Science, 247, 939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brünger, A.4    Yamizumi, Z.5    Nishimura, S.6    Kim, S.-H.7
  • 29
    • 0030036699 scopus 로고    scopus 로고
    • Formation of a transition state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate and GTPase-activating proteins
    • Mittal, R., Ahmadian, M.R., Goody, R.S. and Wittinghofer, A. (1996) Formation of a transition state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate and GTPase-activating proteins. Science, 273, 115-117.
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, R.S.3    Wittinghofer, A.4
  • 30
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1a and a GTP analogue
    • Nassar, N., Horn, G., Herrmann, C., Scherer, A., McCormick, F. and Wittinghofer, A. (1995) The 2.2 Å crystal structure of the ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature, 375, 554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 32
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr. A, 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 34
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin α complexed with GTPγS
    • Noel, J.P., Hamm, H.E. and Sigler, P.B. (1993) The 2.2 Å crystal structure of transducin α complexed with GTPγS. Nature, 366, 654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 35
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. and Bailey, S. (eds), Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993) Oscillation data reduction program. In Sawyer, L., Isaacs, N. and Bailey, S. (eds), CCP4 Study Weekend: Data Collection and Processing. Daresbury Laboratory, Warrington, UK, pp. 56-62.
    • (1993) CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 36
    • 0025310575 scopus 로고
    • Refined crystal structure of the trisphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E.F. Krengel, U., Petsko, G.A., Goody, R.S., Kabsch, W. and Wittinghofer, A. (1990) Refined crystal structure of the trisphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J., 9, 2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 37
    • 0023721977 scopus 로고
    • Human cDNAs rap1 and rap2 homologous to the Drosophila Dras3 encode proteins closely related to ras in the 'effector' region
    • Pizon, V., Chardin, P., Lerosey, I., Olofsson, B. and Tavitian, A. (1988) Human cDNAs rap1 and rap2 homologous to the Drosophila Dras3 encode proteins closely related to ras in the 'effector' region. Oncogene, 3, 201-204
    • (1988) Oncogene , vol.3 , pp. 201-204
    • Pizon, V.1    Chardin, P.2    Lerosey, I.3    Olofsson, B.4    Tavitian, A.5
  • 38
    • 0027285320 scopus 로고
    • ras with GAP, exchange factors, and its biological effector target
    • ras with GAP, exchange factors, and its biological effector target. J. Biol. Chem., 268, 9157-9160.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9157-9160
    • Polakis, P.1    McCormick, F.2
  • 40
    • 0027362032 scopus 로고
    • Prenylation of rab5 is dependent on guanine nucleotide binding
    • Sanford, J.C., Pan, Y. and Wessling-Resnik, M. (1993) Prenylation of rab5 is dependent on guanine nucleotide binding. J. Biol. Chem., 268, 22773-22776.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22773-22776
    • Sanford, J.C.1    Pan, Y.2    Wessling-Resnik, M.3
  • 41
    • 0029829561 scopus 로고    scopus 로고
    • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with ras
    • Scheffzek, K., Lautwein, A., Kabsch, W., Reza Ahmadian, M. and Wittinghofer, A. (1996) Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with ras. Nature, 384, 591-596.
    • (1996) Nature , vol.384 , pp. 591-596
    • Scheffzek, K.1    Lautwein, A.2    Kabsch, W.3    Reza Ahmadian, M.4    Wittinghofer, A.5
  • 43
    • 0028848502 scopus 로고
    • Nucleotide induced conformation determines post translational isoprenylation of the ras related rab6 protein in insect cells
    • Schiedel, A.C., Barnekow, A. and Mayer, T. (1995) Nucleotide induced conformation determines post translational isoprenylation of the ras related rab6 protein in insect cells. FEBS Lett., 376, 113-119.
    • (1995) FEBS Lett. , vol.376 , pp. 113-119
    • Schiedel, A.C.1    Barnekow, A.2    Mayer, T.3
  • 44
    • 0025275582 scopus 로고
    • Time-resolved X-ray crystallography study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis
    • Schlichting, I. et al. (1990) Time-resolved X-ray crystallography study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis. Nature, 345, 309-315
    • (1990) Nature , vol.345 , pp. 309-315
    • Schlichting, I.1
  • 46
    • 0023697249 scopus 로고
    • p21-ras effector domain mutants constructed by 'cassette' mutagenesis
    • Stone, J., Vass, W., Wilumsen, B. and Lowy, D. (1988) p21-ras effector domain mutants constructed by 'cassette' mutagenesis. Mol. Cell. Biol., 8, 3565-3569.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3565-3569
    • Stone, J.1    Vass, W.2    Wilumsen, B.3    Lowy, D.4
  • 49
    • 0025908897 scopus 로고
    • The ras protein family: Evolutionary tree and role of conserved amino acids
    • Valencia, A., Chardin, P., Wittinghofer, A. and Sander, C. (1991) The ras protein family: evolutionary tree and role of conserved amino acids. Biochemistry, 30, 4637-4648.
    • (1991) Biochemistry , vol.30 , pp. 4637-4648
    • Valencia, A.1    Chardin, P.2    Wittinghofer, A.3    Sander, C.4
  • 52
    • 0030464444 scopus 로고    scopus 로고
    • How Ras-related proteins talk to their effectors
    • Wittinghofer, A. and Nassar, N. (1996) How Ras-related proteins talk to their effectors. Trends Biochem. Sci., 21, 488-491.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 488-491
    • Wittinghofer, A.1    Nassar, N.2
  • 53
    • 0030446448 scopus 로고    scopus 로고
    • Structural insights into the function of the rab GDI superfamily
    • Wu, S.-K., Zeng, K., Wilson, I.A. and Balch, W.E. (1996) Structural insights into the function of the rab GDI superfamily. Trends Biochem. Sci., 21, 472-476.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 472-476
    • Wu, S.-K.1    Zeng, K.2    Wilson, I.A.3    Balch, W.E.4
  • 54
    • 0028049166 scopus 로고
    • Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein
    • Yamasaki, K. et al. (1994) Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein. Biochemistry, 33, 65-73.
    • (1994) Biochemistry , vol.33 , pp. 65-73
    • Yamasaki, K.1


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