메뉴 건너뛰기




Volumn 27, Issue 2, 1997, Pages 315-318

Crystallization and preliminary X-ray crystallographic study of the Ras- GTPase-activating domain of human p120GAP

Author keywords

catalytic domain; cross linking; hanging drop; p21; seeding

Indexed keywords

GROWTH ASSOCIATED PROTEIN; GUANOSINE TRIPHOSPHATASE; RAS PROTEIN;

EID: 0031042009     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199702)27:2<315::AID-PROT17>3.0.CO;2-P     Document Type: Article
Times cited : (9)

References (47)
  • 3
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H.R., Sanders, D.A., McCormick, F. The GTPase superfamily: A conserved switch for diverse 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
  • 4
    • 0025740753 scopus 로고
    • The structure of ras protein: A model for a universal molecular switch
    • Wittinghofer, A., Pai, E. The structure of ras protein: A model for a universal molecular switch. TIBS 16:383-387, 1991.
    • (1991) TIBS , vol.16 , pp. 383-387
    • Wittinghofer, A.1    Pai, E.2
  • 6
    • 0029089593 scopus 로고
    • Ras-effector interactions, the problem of specificity
    • Wittinghofer, A., Herrmann, C. Ras-effector interactions, the problem of specificity. FEBS Lett. 369:52-56, 1995.
    • (1995) FEBS Lett. , vol.369 , pp. 52-56
    • Wittinghofer, A.1    Herrmann, C.2
  • 7
    • 0027201548 scopus 로고
    • GTP-dependent association of Raf-1 with Ha-Ras: Identification of Raf as a target downstream of Ras in mammalian cells
    • Koide, H., Satoh, T., Nakafuku, M., Kaziro, Y. GTP-dependent association of Raf-1 with Ha-Ras: Identification of Raf as a target downstream of Ras in mammalian cells. Proc. Natl. Acad. Sci. USA 90:8683-8686, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8683-8686
    • Koide, H.1    Satoh, T.2    Nakafuku, M.3    Kaziro, Y.4
  • 8
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A.B., Hollenberg, S.M., Cooper, J.A. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214, 1993.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 9
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne, P.H., Rodriguez Viciana, P. Downward, J. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 364:352-355, 1993.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Rodriguez Viciana, P.2    Downward, J.3
  • 12
    • 0027337519 scopus 로고
    • Complexes of Ras GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie, S.A., Willumsen, B.M., Weber, M.J., Wolfman, A. Complexes of Ras GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 260:1658-1661, 1993.
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 14
    • 0028153277 scopus 로고
    • Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator
    • Hofer, F., Fields, S., Schneider, C., Martin, G.S. Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator. Proc. Natl. Acad. Sci. USA 91:11089-11093, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11089-11093
    • Hofer, F.1    Fields, S.2    Schneider, C.3    Martin, G.S.4
  • 17
    • 0026711081 scopus 로고
    • Mutational and kinetic analysis of the GTPase-activating protein (GAP)-p21 interaction: The C-terminal domain of GAP is not sufficient for full activity
    • Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J.E., Wittinghofer, A. Mutational and kinetic analysis of the GTPase-activating protein (GAP)-p21 interaction: The C-terminal domain of GAP is not sufficient for full activity. Mol. Cell. Biol. 12:2050-2056, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2050-2056
    • Gideon, P.1    John, J.2    Frech, M.3    Lautwein, A.4    Clark, R.5    Scheffler, J.E.6    Wittinghofer, A.7
  • 18
    • 0027765499 scopus 로고
    • Kinetics of interaction between normal and proline 12 Ras and the GTPase-activating proteins, p120-GAP and neurofibromin
    • Eccleston, J.F., Moore, K.J.M., Morgan, L., Skinner, R.H., Lowe, P.N. Kinetics of interaction between normal and proline 12 Ras and the GTPase-activating proteins, p120-GAP and neurofibromin. J. Biol. Chem. 268:27012-27019, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27012-27019
    • Eccleston, J.F.1    Moore, K.J.M.2    Morgan, L.3    Skinner, R.H.4    Lowe, P.N.5
  • 19
    • 0023619575 scopus 로고
    • A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants
    • Trahey, M., McCormick, F. A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. Science 238:542-545, 1987.
    • (1987) Science , vol.238 , pp. 542-545
    • Trahey, M.1    McCormick, F.2
  • 23
    • 0025201012 scopus 로고
    • The NF1 locus encodes a protein functionally related to mammalian GAP and yeast IRa proteins
    • Ballester, R., Marchuk, D., Boguski, M., Saulino, A., Letcher, R., Wigler, M., Collins, F. The NF1 locus encodes a protein functionally related to mammalian GAP and yeast IRA proteins. Cell 63:851-859, 1991.
    • (1991) Cell , vol.63 , pp. 851-859
    • Ballester, R.1    Marchuk, D.2    Boguski, M.3    Saulino, A.4    Letcher, R.5    Wigler, M.6    Collins, F.7
  • 29
    • 0024497239 scopus 로고
    • IRA1, an inhibitory regulator of the RAS-cyclic AMP pathway in Saccharomyces cerevisiae
    • Tanaka, K., Matsumoto, K., Toh-e, A. IRA1, an inhibitory regulator of the RAS-cyclic AMP pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:757-768, 1989.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 757-768
    • Tanaka, K.1    Matsumoto, K.2    Toh-e, A.3
  • 30
    • 0025283632 scopus 로고
    • IRA2, a second gene of Saccharomyces cerevisiae that encodes a protein with a domain homologous to mammalian ras GTPase-activating protein
    • Tanaka, K., Nakafuku, M., Tamanoi, F., Kaziro, Y., Matsumoto, K., Toh-e, A. IRA2, a second gene of Saccharomyces cerevisiae that encodes a protein with a domain homologous to mammalian ras GTPase-activating protein. Mol. Cell. Biol. 10:4303-4313, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4303-4313
    • Tanaka, K.1    Nakafuku, M.2    Tamanoi, F.3    Kaziro, Y.4    Matsumoto, K.5    Toh-e, A.6
  • 31
    • 0026588783 scopus 로고
    • A putative ras GTPase activating protein acts as a negative regulator of signalling by the sevenless receptor tyrosine kinase
    • Gaul, U., Mardon, G., Rubin, G.M. A putative ras GTPase activating protein acts as a negative regulator of signalling by the sevenless receptor tyrosine kinase. Cell 68:1007-1019, 1992.
    • (1992) Cell , vol.68 , pp. 1007-1019
    • Gaul, U.1    Mardon, G.2    Rubin, G.M.3
  • 32
    • 0025806672 scopus 로고
    • Byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype
    • Wang, Y., Xu, H.-P., Riggs, M., Rodgers, L., Wigler, M. byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype. Mol. Cell. Biol. 11:3554-3563, 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3554-3563
    • Wang, Y.1    Xu, H.-P.2    Riggs, M.3    Rodgers, L.4    Wigler, M.5
  • 40
    • 0029120950 scopus 로고
    • Loss of neurofibromin results in neurotrophin-independent survival of embryonic sensory and sympathetic neurons
    • Vogel, K.S., Brannan, C.I., Jenkins, N.A., Copeland, N.G., Parada, L.F. Loss of neurofibromin results in neurotrophin-independent survival of embryonic sensory and sympathetic neurons. Cell 82:733-742, 1995.
    • (1995) Cell , vol.82 , pp. 733-742
    • Vogel, K.S.1    Brannan, C.I.2    Jenkins, N.A.3    Copeland, N.G.4    Parada, L.F.5
  • 41
    • 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, K.S., Wittinghofer, A. Formation of a transition state analog of the Ras GTPase reaction by Ras · GDP, tetrafluoroaluminate and GTPase-activating proteins. Science 273:115-117, 1996.
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, K.S.3    Wittinghofer, A.4
  • 42
    • 0023777735 scopus 로고
    • Tightly regulated tac promoters useful for the expression of unfused and fused proteins in Escherichia coli
    • Amman, E., Ochs, B., Abel, K.-J. Tightly regulated tac promoters useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315, 1988.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amman, E.1    Ochs, B.2    Abel, K.-J.3
  • 43
    • 36149068929 scopus 로고
    • Optically focusing x-ray diffraction camera
    • Franks, A. Optically focusing x-ray diffraction camera. Proc. Phys. Soc. Lond. [B]68:1054-1064, 1955
    • (1955) Proc. Phys. Soc. Lond. , vol.B68 , pp. 1054-1064
    • Franks, A.1
  • 44
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:795-800, 1993.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 47
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski, J., Wang, J., Steitz, T.A., Moore, P.B. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13:3661-3668, 1994.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.