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Volumn 403, Issue 6769, 2000, Pages 567-571

Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; RAS PROTEIN;

EID: 0034598734     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35000617     Document Type: Article
Times cited : (274)

References (30)
  • 1
    • 0020955866 scopus 로고
    • Interferon induction of fibroblast proteins with guanylate binding activity
    • Cheng, Y.-S. E., Colonno, R. J. & Yin, F. H. Interferon induction of fibroblast proteins with guanylate binding activity J. Biol. Chem. 258, 7746-7750 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 7746-7750
    • Cheng, Y.-S.E.1    Colonno, R.J.2    Yin, F.H.3
  • 2
    • 0025900442 scopus 로고
    • Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP
    • Cheng, Y.-S. E., Patterson, C. E. & Staeheli, P. Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP Mol. Cell. Biol. 11, 4717-4725 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4717-4725
    • Cheng, Y.-S.E.1    Patterson, C.E.2    Staeheli, P.3
  • 3
    • 0028243476 scopus 로고
    • The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP
    • Schwemmle, M. & Staeheli, P. The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP J. biol. Chem. 269, 11299-11305 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 11299-11305
    • Schwemmle, M.1    Staeheli, P.2
  • 4
    • 0033616531 scopus 로고    scopus 로고
    • Interferon-induced guanylate-binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalo-myocarditis virus
    • Anderson, S. L., Carton, J. M., Lou, J., Xing, L. & Rubin, B. Y. Interferon-induced guanylate-binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalo-myocarditis virus Virology 256, 8-14 (1999).
    • (1999) Virology , vol.256 , pp. 8-14
    • Anderson, S.L.1    Carton, J.M.2    Lou, J.3    Xing, L.4    Rubin, B.Y.5
  • 5
    • 0033105560 scopus 로고    scopus 로고
    • Functional diversity in the dynamin family
    • van der Bliek, A. M. Functional diversity in the dynamin family Trends Cell Biol. 9, 96-102 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 96-102
    • Van Der Bliek, A.M.1
  • 6
    • 0032534733 scopus 로고    scopus 로고
    • Two families of GTPases dominate the complex cellular response to IFN-γ
    • Boehm, U. et al. Two families of GTPases dominate the complex cellular response to IFN-γ J. Immunol. 161, 6715-6723 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 6715-6723
    • Boehm, U.1
  • 7
  • 8
    • 0033578805 scopus 로고    scopus 로고
    • Nucleotide-binding characteristics of human guanylate-binding protein 1 and identification of the third canonical GTP-binding motif
    • Praefcke, G. J. K., Geyer, M., Schwemmle, M., Kalbitzer, H. R. & Herrmann, C. Nucleotide-binding characteristics of human guanylate-binding protein 1 and identification of the third canonical GTP-binding motif J. Mol. Biol. 292, 321-332 (1999)
    • (1999) J. Mol. Biol. , vol.292 , pp. 321-332
    • Praefcke, G.J.K.1    Geyer, M.2    Schwemmle, M.3    Kalbitzer, H.R.4    Herrmann, C.5
  • 9
    • 0027418991 scopus 로고
    • Towards a model for the interaction between elongation factor Tu and the ribosome
    • Weijland, A. & Parmeggiani, A. Towards a model for the interaction between elongation factor Tu and the ribosome Science 259, 1311-1314 (1993)
    • (1993) Science , vol.259 , pp. 1311-1314
    • Weijland, A.1    Parmeggiani, A.2
  • 10
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP-and GTP-binding proteins
    • Saraste, M., Sibbald, P. R. & Wittinghofer, A. The P-loop - a common motif in ATP-and GTP-binding proteins Trends. Biochem. Sci. 15, 430-434 (1990).
    • (1990) Trends. Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 12
    • 0032127912 scopus 로고    scopus 로고
    • GTPase activating proteins: Helping hands to complement an active site
    • Scheffzek, K., Ahmadian, M. R. & Wittinghofer, A. GTPase activating proteins: helping hands to complement an active site Trends Biochem. Sci. 23, 257-262 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 13
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self-assembly stimulates its GTPase activity
    • Warnock, D. E., Hinshaw, J. E. & Schmid, S. L. Dynamin self-assembly stimulates its GTPase activity J. Biol. Chem. 271, 22310-22314 (1996)
    • (1996) J. Biol. Chem. , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 14
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
    • Sever, S., Muhlberg, A. B. & Schmid, S. L. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature 398, 481-486 (1999).
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3
  • 15
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell, M. H. B., Marks, B., Wigge, P. & McMahon, H. T. Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring Nature Cell Biol. 1, 27-32 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 27-32
    • Stowell, M.H.B.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 16
    • 0029036975 scopus 로고
    • Unexpected structural requirements for GTPase activity of the interferon-induced MxA protein
    • Schwemmle, M., Richter, M. F., Herrmann, C., Nassar, N. & Staeheli, P. Unexpected structural requirements for GTPase activity of the interferon-induced MxA protein J. Biol. Chem. 270, 13518-13523 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13518-13523
    • Schwemmle, M.1    Richter, M.F.2    Herrmann, C.3    Nassar, N.4    Staeheli, P.5
  • 17
    • 0032561212 scopus 로고    scopus 로고
    • Domains mediating intramolecular folding and oligomerization of MxA GTPase
    • Schumacher, B. & Staeheli, P. Domains mediating intramolecular folding and oligomerization of MxA GTPase J. Biol. Chem. 273, 28365-28370 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 28365-28370
    • Schumacher, B.1    Staeheli, P.2
  • 18
  • 19
    • 0033537976 scopus 로고    scopus 로고
    • Multiple distinct coiled-coils are involved in dynamin self-assembly
    • Okamoto, P. M., Tripet, B., Litowski, J., Hodges, R. S. & Vallee, R. B. Multiple distinct coiled-coils are involved in dynamin self-assembly J. Biol. Chem. 274, 10277-10286 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10277-10286
    • Okamoto, P.M.1    Tripet, B.2    Litowski, J.3    Hodges, R.S.4    Vallee, R.B.5
  • 20
    • 0028103275 scopus 로고
    • N.4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational project, N.4. The CCP4 suite: programs for protein crystallography Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 21
    • 0033548268 scopus 로고    scopus 로고
    • GTP-bound human MxA protein interacts with the nucleocapsids of thogoto virus (Orthomyxoviridae)
    • Kochs, G. & Haller, O. GTP-bound Human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae) J. Biol. Chem. 274, 4370-4376 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 4370-4376
    • Kochs, G.1    Haller, O.2
  • 22
    • 0030499814 scopus 로고    scopus 로고
    • Correlated phasing of multiple isomorphous replacement data
    • Terwilliger, T. C. & Berendzen, J. Correlated phasing of multiple isomorphous replacement data Acta Crystallogr. D 52, 749-757 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 749-757
    • Terwilliger, T.C.1    Berendzen, J.2
  • 23
    • 0030809260 scopus 로고    scopus 로고
    • wARP:Improvement and extension of crystallographic phases by weighted averaging of multiple refined dummy atomic models
    • Perrakis, A., Sixma, T. K., Wilson, K. S. & Lamzin, V. S. wARP:improvement and extension of crystallographic phases by weighted averaging of multiple refined dummy atomic models Acta Crystallogr. D 53, 448-455 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 24
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones, T. A. & Kjeldgaard, M. Electron-density map interpretation Methods Enzymol. 277, 173-208 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 25
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software system for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography and NMR system: a new software system for macromolecular structure determination Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 26
    • 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 J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 27
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merrit, E. A. & Murphy, M. E. P. Raster3D version 2.0. A program for photorealistic molecular graphics Acta Crystallogr. D 50, 869-873 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11, 281-296 (1991)
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22, 2577-2637 (1983)
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35Ȧ resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F. et at. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35Ȧ 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.