메뉴 건너뛰기




Volumn 109, Issue 12, 2015, Pages 2602-2613

High-Affinity Interaction of the K-Ras4B Hypervariable Region with the Ras Active Site

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PEPTIDE FRAGMENT; PROTEIN BINDING; PROTEIN P21; RAS PROTEIN;

EID: 84948464277     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.09.034     Document Type: Article
Times cited : (68)

References (56)
  • 2
    • 74449093973 scopus 로고    scopus 로고
    • A comprehensive catalogue of somatic mutations from a human cancer genome
    • E.D. Pleasance, and R.K. Cheetham M.R. Stratton A comprehensive catalogue of somatic mutations from a human cancer genome Nature 463 2010 191 196
    • (2010) Nature , vol.463 , pp. 191-196
    • Pleasance, E.D.1    Cheetham, R.K.2    Stratton, M.R.3
  • 3
    • 84861147473 scopus 로고    scopus 로고
    • A comprehensive survey of Ras mutations in cancer
    • I.A. Prior, P.D. Lewis, and C. Mattos A comprehensive survey of Ras mutations in cancer Cancer Res. 72 2012 2457 2467
    • (2012) Cancer Res. , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 5
    • 0025275582 scopus 로고
    • Time-resolved x-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis
    • I. Schlichting, and S.C. Almo R.S. Goody Time-resolved x-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis Nature 345 1990 309 315
    • (1990) Nature , vol.345 , pp. 309-315
    • Schlichting, I.1    Almo, S.C.2    Goody, R.S.3
  • 6
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • K. Scheffzek, and M.R. Ahmadian A. Wittinghofer The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants Science 277 1997 333 338
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 7
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • A. Wittinghofer, and I.R. Vetter Structure-function relationships of the G domain, a canonical switch motif Annu. Rev. Biochem. 80 2011 943 971
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 9
    • 84859463451 scopus 로고    scopus 로고
    • Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity
    • T. Maurer, and L.S. Garrenton G. Fang Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity Proc. Natl. Acad. Sci. USA 109 2012 5299 5304
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5299-5304
    • Maurer, T.1    Garrenton, L.S.2    Fang, G.3
  • 10
    • 84888639050 scopus 로고    scopus 로고
    • K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
    • J.M. Ostrem, and U. Peters K.M. Shokat K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions Nature 503 2013 548 551
    • (2013) Nature , vol.503 , pp. 548-551
    • Ostrem, J.M.1    Peters, U.2    Shokat, K.M.3
  • 11
    • 84862649997 scopus 로고    scopus 로고
    • Discovery of small molecules that bind to K-Ras and inhibit Sos-mediated activation
    • Q. Sun, and J.P. Burke S.W. Fesik Discovery of small molecules that bind to K-Ras and inhibit Sos-mediated activation Angew. Chem. Int. Ed. Engl. 51 2012 6140 6143
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 6140-6143
    • Sun, Q.1    Burke, J.P.2    Fesik, S.W.3
  • 12
    • 84865463399 scopus 로고    scopus 로고
    • Ras inhibition via direct Ras binding - Is there a path forward?
    • W. Wang, G. Fang, and J. Rudolph Ras inhibition via direct Ras binding - is there a path forward? Bioorg. Med. Chem. Lett. 22 2012 5766 5776
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 5766-5776
    • Wang, W.1    Fang, G.2    Rudolph, J.3
  • 13
    • 84886948259 scopus 로고    scopus 로고
    • Pathway drug cocktail: Targeting Ras signaling based on structural pathways
    • R. Nussinov, C.J. Tsai, and C. Mattos 'Pathway drug cocktail': targeting Ras signaling based on structural pathways Trends Mol. Med. 19 2013 695 704
    • (2013) Trends Mol. Med. , vol.19 , pp. 695-704
    • Nussinov, R.1    Tsai, C.J.2    Mattos, C.3
  • 14
    • 79960051265 scopus 로고    scopus 로고
    • Therapeutic strategies for targeting Ras proteins
    • S. Gysin, and M. Salt F. McCormick Therapeutic strategies for targeting Ras proteins Genes Cancer 2 2011 359 372
    • (2011) Genes Cancer , vol.2 , pp. 359-372
    • Gysin, S.1    Salt, M.2    McCormick, F.3
  • 15
    • 84886745490 scopus 로고    scopus 로고
    • US National Cancer Institute's new Ras project targets an old foe
    • H. Thompson US National Cancer Institute's new Ras project targets an old foe Nat. Med. 19 2013 949 950
    • (2013) Nat. Med. , vol.19 , pp. 949-950
    • Thompson, H.1
  • 16
    • 84878838220 scopus 로고    scopus 로고
    • Fixing a hole where the Ras gets in
    • J.S. Iwig, and J. Kuriyan Fixing a hole where the Ras gets in Cell 153 2013 1191 1193
    • (2013) Cell , vol.153 , pp. 1191-1193
    • Iwig, J.S.1    Kuriyan, J.2
  • 17
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • M.D. Resh Membrane targeting of lipid modified signal transduction proteins Subcell. Biochem. 37 2004 217 232
    • (2004) Subcell. Biochem. , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 18
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • J.F. Hancock, H. Paterson, and C.J. Marshall A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane Cell 63 1990 133 139
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 19
    • 84255195028 scopus 로고    scopus 로고
    • Regulating the regulator: Post-translational modification of RAS
    • I.M. Ahearn, and K. Haigis M.R. Philips Regulating the regulator: post-translational modification of RAS Nat. Rev. Mol. Cell Biol. 13 2012 39 51
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 39-51
    • Ahearn, I.M.1    Haigis, K.2    Philips, M.R.3
  • 20
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • D. Abankwa, and A.A. Gorfe J.F. Hancock Ras membrane orientation and nanodomain localization generate isoform diversity Proc. Natl. Acad. Sci. USA 107 2010 1130 1135
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1130-1135
    • Abankwa, D.1    Gorfe, A.A.2    Hancock, J.F.3
  • 21
    • 65349150639 scopus 로고    scopus 로고
    • Isoform-specific Ras functions in development and cancer
    • M.P. Quinlan, and J. Settleman Isoform-specific Ras functions in development and cancer Future Oncol. 5 2009 105 116
    • (2009) Future Oncol. , vol.5 , pp. 105-116
    • Quinlan, M.P.1    Settleman, J.2
  • 22
    • 79960038169 scopus 로고    scopus 로고
    • Functional specificity of Ras isoforms: So similar but so different
    • E. Castellano, and E. Santos Functional specificity of Ras isoforms: so similar but so different Genes Cancer 2 2011 216 231
    • (2011) Genes Cancer , vol.2 , pp. 216-231
    • Castellano, E.1    Santos, E.2
  • 23
    • 84927144988 scopus 로고    scopus 로고
    • Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region
    • H. Jang, and S.J. Abraham V. Gaponenko Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region J. Biol. Chem. 290 2015 9465 9477
    • (2015) J. Biol. Chem. , vol.290 , pp. 9465-9477
    • Jang, H.1    Abraham, S.J.2    Gaponenko, V.3
  • 24
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic Ras proteins
    • M.V. Milburn, and L. Tong S.H. Kim Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic Ras proteins Science 247 1990 939 945
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    Kim, S.H.3
  • 26
    • 79953690491 scopus 로고    scopus 로고
    • Peptide structure stabilization by membrane anchoring and its general applicability to the development of potent cell-permeable inhibitors
    • L. Johannessen, and J. Remsberg N.I. Tarasova Peptide structure stabilization by membrane anchoring and its general applicability to the development of potent cell-permeable inhibitors ChemBioChem 12 2011 914 921
    • (2011) ChemBioChem , vol.12 , pp. 914-921
    • Johannessen, L.1    Remsberg, J.2    Tarasova, N.I.3
  • 27
    • 77955417069 scopus 로고    scopus 로고
    • Expression, purification, and characterization of soluble K-Ras4B for structural analysis
    • S.J. Abraham, and I. Muhamed V. Gaponenko Expression, purification, and characterization of soluble K-Ras4B for structural analysis Protein Expr. Purif. 73 2010 125 131
    • (2010) Protein Expr. Purif. , vol.73 , pp. 125-131
    • Abraham, S.J.1    Muhamed, I.2    Gaponenko, V.3
  • 29
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 30
    • 84986512474 scopus 로고
    • CHARMM - A program for macromolecular energy, minimization, and dynamics calculations
    • B.R. Brooks, and R.E. Bruccoleri M. Karplus CHARMM - a program for macromolecular energy, minimization, and dynamics calculations J. Comput. Chem. 4 1983 187 217
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1    Bruccoleri, R.E.2    Karplus, M.3
  • 31
    • 0038713404 scopus 로고    scopus 로고
    • Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics
    • P. Grayson, E. Tajkhorshid, and K. Schulten Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics Biophys. J. 85 2003 36 48
    • (2003) Biophys. J. , vol.85 , pp. 36-48
    • Grayson, P.1    Tajkhorshid, E.2    Schulten, K.3
  • 34
    • 33751157933 scopus 로고
    • Solvent-induced forces between two hydrophilic groups
    • S.R. Durell, B.R. Brooks, and A. Bennaim Solvent-induced forces between two hydrophilic groups J. Phys. Chem. 98 1994 2198 2202
    • (1994) J. Phys. Chem. , vol.98 , pp. 2198-2202
    • Durell, S.R.1    Brooks, B.R.2    Bennaim, A.3
  • 35
    • 84922069121 scopus 로고    scopus 로고
    • A novel method for the production of fully modified K-Ras 4B
    • T.S. Chavan, and J.O. Meyer V. Gaponenko A novel method for the production of fully modified K-Ras 4B Methods Mol. Biol. 1120 2014 19 32
    • (2014) Methods Mol. Biol. , vol.1120 , pp. 19-32
    • Chavan, T.S.1    Meyer, J.O.2    Gaponenko, V.3
  • 36
    • 68849095670 scopus 로고    scopus 로고
    • The hypervariable region of K-Ras4B is responsible for its specific interactions with calmodulin
    • S.J. Abraham, and R.P. Nolet V. Gaponenko The hypervariable region of K-Ras4B is responsible for its specific interactions with calmodulin Biochemistry 48 2009 7575 7583
    • (2009) Biochemistry , vol.48 , pp. 7575-7583
    • Abraham, S.J.1    Nolet, R.P.2    Gaponenko, V.3
  • 38
    • 84884497350 scopus 로고    scopus 로고
    • Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions
    • S.A. Seidel, and P.M. Dijkman S. Duhr Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions Methods 59 2013 301 315
    • (2013) Methods , vol.59 , pp. 301-315
    • Seidel, S.A.1    Dijkman, P.M.2    Duhr, S.3
  • 40
    • 33846066294 scopus 로고    scopus 로고
    • CAMP activation of PKA defines an ancient signaling mechanism
    • R. Das, and V. Esposito G. Melacini cAMP activation of PKA defines an ancient signaling mechanism Proc. Natl. Acad. Sci. USA 104 2007 93 98
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 93-98
    • Das, R.1    Esposito, V.2    Melacini, G.3
  • 42
    • 0028795913 scopus 로고
    • Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase
    • C. Herrmann, G.A. Martin, and A. Wittinghofer Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase J. Biol. Chem. 270 1995 2901 2905
    • (1995) J. Biol. Chem. , vol.270 , pp. 2901-2905
    • Herrmann, C.1    Martin, G.A.2    Wittinghofer, A.3
  • 43
    • 0034698068 scopus 로고    scopus 로고
    • Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions
    • J.G. Williams, and J.K. Drugan S.L. Campbell Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions J. Biol. Chem. 275 2000 22172 22179
    • (2000) J. Biol. Chem. , vol.275 , pp. 22172-22179
    • Williams, J.G.1    Drugan, J.K.2    Campbell, S.L.3
  • 44
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • M.S. Boguski, and F. McCormick Proteins regulating Ras and its relatives Nature 366 1993 643 654
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 45
    • 84894039820 scopus 로고    scopus 로고
    • Integrated RAS signaling defined by parallel NMR detection of effectors and regulators
    • M.J. Smith, and M. Ikura Integrated RAS signaling defined by parallel NMR detection of effectors and regulators Nat. Chem. Biol. 10 2014 223 230
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 223-230
    • Smith, M.J.1    Ikura, M.2
  • 46
    • 0029007101 scopus 로고
    • The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch
    • P.A. Randazzo, and T. Terui R.A. Kahn The myristoylated amino terminus of ADP-ribosylation factor 1 is a phospholipid- and GTP-sensitive switch J. Biol. Chem. 270 1995 14809 14815
    • (1995) J. Biol. Chem. , vol.270 , pp. 14809-14815
    • Randazzo, P.A.1    Terui, T.2    Kahn, R.A.3
  • 47
    • 52049115702 scopus 로고    scopus 로고
    • Dissociation of Rac1(GDP)·RhoGDI complexes by the cooperative action of anionic liposomes containing phosphatidylinositol 3,4,5-trisphosphate, Rac guanine nucleotide exchange factor, and GTP
    • Y. Ugolev, and Y. Berdichevsky E. Pick Dissociation of Rac1(GDP)·RhoGDI complexes by the cooperative action of anionic liposomes containing phosphatidylinositol 3,4,5-trisphosphate, Rac guanine nucleotide exchange factor, and GTP J. Biol. Chem. 283 2008 22257 22271
    • (2008) J. Biol. Chem. , vol.283 , pp. 22257-22271
    • Ugolev, Y.1    Berdichevsky, Y.2    Pick, E.3
  • 48
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • J. Yan, and S. Roy J.F. Hancock Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase J. Biol. Chem. 273 1998 24052 24056
    • (1998) J. Biol. Chem. , vol.273 , pp. 24052-24056
    • Yan, J.1    Roy, S.2    Hancock, J.F.3
  • 49
    • 0031917171 scopus 로고    scopus 로고
    • Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo
    • M.K. Jones, and J.H. Jackson Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo J. Biol. Chem. 273 1998 1782 1787
    • (1998) J. Biol. Chem. , vol.273 , pp. 1782-1787
    • Jones, M.K.1    Jackson, J.H.2
  • 50
    • 6344234904 scopus 로고    scopus 로고
    • NMR characterization of full-length farnesylated and non-farnesylated H-Ras and its implications for Raf activation
    • R. Thapar, J.G. Williams, and S.L. Campbell NMR characterization of full-length farnesylated and non-farnesylated H-Ras and its implications for Raf activation J. Mol. Biol. 343 2004 1391 1408
    • (2004) J. Mol. Biol. , vol.343 , pp. 1391-1408
    • Thapar, R.1    Williams, J.G.2    Campbell, S.L.3
  • 51
    • 79951495657 scopus 로고    scopus 로고
    • Identification of H-Ras-specific motif for the activation of invasive signaling program in human breast epithelial cells
    • H.Y. Yong, and J.S. Hwang A. Moon Identification of H-Ras-specific motif for the activation of invasive signaling program in human breast epithelial cells Neoplasia 13 2011 98 107
    • (2011) Neoplasia , vol.13 , pp. 98-107
    • Yong, H.Y.1    Hwang, J.S.2    Moon, A.3
  • 52
    • 84948469412 scopus 로고    scopus 로고
    • GTP binding and oncogenic mutations may attenuate hypervariable region (HVR)-catalytic domain interactions in small GTPase KRAS4B, exposing the effector finding site
    • Published online October 9, 2015
    • S. Lu, and A. Banerjee R. Nussinov GTP binding and oncogenic mutations may attenuate hypervariable region (HVR)-catalytic domain interactions in small GTPase KRAS4B, exposing the effector finding site J. Biol. Chem. 2015 10.1074/jbc.M115.664755 Published online October 9, 2015
    • (2015) J. Biol. Chem.
    • Lu, S.1    Banerjee, A.2    Nussinov, R.3
  • 53
    • 0028584355 scopus 로고
    • Polylysine domain of K-ras 4B protein is crucial for malignant transformation
    • J.H. Jackson, and J.W. Li C.G. Cochrane Polylysine domain of K-ras 4B protein is crucial for malignant transformation Proc. Natl. Acad. Sci. USA 91 1994 12730 12734
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12730-12734
    • Jackson, J.H.1    Li, J.W.2    Cochrane, C.G.3
  • 54
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • D. Frishman, and P. Argos Knowledge-based protein secondary structure assignment Proteins 23 1995 566 579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 56
    • 0034645726 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95
    • H. Tochio, and F. Hung M. Zhang Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95 J. Mol. Biol. 295 2000 225 237
    • (2000) J. Mol. Biol. , vol.295 , pp. 225-237
    • Tochio, H.1    Hung, F.2    Zhang, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.