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Volumn 21, Issue 4, 2012, Pages 583-588

Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin

Author keywords

Crystallography; Cytoskeleton; Focal adhesion; Protein protein interaction

Indexed keywords

INTEGRIN; TALIN; VINCULIN;

EID: 84858689928     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2041     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 67650288199 scopus 로고    scopus 로고
    • Biochemical and structural properties of the integrin-associated cytoskeletal protein talin
    • Critchley DR (2009) Biochemical and structural properties of the integrin-associated cytoskeletal protein talin. Annual Rev Biophys 38:235-254.
    • (2009) Annual Rev Biophys , vol.38 , pp. 235-254
    • Critchley, D.R.1
  • 2
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood DA (2004) Integrin activation. J Cell Sci 117:657-666.
    • (2004) J Cell Sci , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 3
    • 0033213922 scopus 로고    scopus 로고
    • The Talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH (1999) The Talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation. J Biol Chem 274:28071-28074.
    • (1999) J Biol Chem , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 6
    • 33744829519 scopus 로고    scopus 로고
    • An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton
    • DOI 10.1038/ncb1411, PII N1411
    • Tanentzapf G, Brown NH (2006) An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton. Nat Cell Biol 8:601-606. (Pubitemid 43827353)
    • (2006) Nature Cell Biology , vol.8 , Issue.6 , pp. 601-606
    • Tanentzapf, G.1    Brown, N.H.2
  • 7
    • 3142526378 scopus 로고    scopus 로고
    • Crystal structure of human vinculin
    • DOI 10.1016/j.str.2004.05.009, PII S0969212604002023
    • Borgon RA, Vonrhein C, Bricogne G, Bois PR, Izard T (2004) Crystal structure of human vinculin. Structure 12:1189-1197. (Pubitemid 38900761)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1189-1197
    • Borgon, R.A.1    Vonrhein, C.2    Bricogne, G.3    Bois, P.R.J.4    Izard, T.5
  • 8
    • 77956289735 scopus 로고    scopus 로고
    • A helix replacement mechanism directs metavinculin functions
    • Rangarajan ES, Lee JH, Yogesha SD, Izard T (2010) A helix replacement mechanism directs metavinculin functions. PLoS ONE 5:e10679.
    • (2010) PLoS ONE , vol.5
    • Rangarajan, E.S.1    Lee, J.H.2    Yogesha, S.D.3    Izard, T.4
  • 9
    • 0347717894 scopus 로고    scopus 로고
    • Vinculin activation by talin through helical bundle conversion
    • DOI 10.1038/nature02281
    • Izard T, Evans G, Borgon RA, Rush CL, Bricogne G, Bois PR (2004) Vinculin activation by talin through helical bundle conversion. Nature 427:171-175. (Pubitemid 38094959)
    • (2004) Nature , vol.427 , Issue.6970 , pp. 171-175
    • Izard, T.1    Evans, G.2    Borgon, R.A.3    Rush, C.L.4    Bricogne, G.5    Bois, P.R.J.6
  • 10
    • 3042600016 scopus 로고    scopus 로고
    • Structural basis for amplifying vinculin activation by talin
    • DOI 10.1074/jbc.M403076200
    • Izard T, Vonrhein C (2004) Structural basis for amplifying vinculin activation by talin. J Biol Chem 279: 27667-27678. (Pubitemid 38812608)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27667-27678
    • Izard, T.1    Vonrhein, C.2
  • 11
    • 79960687699 scopus 로고    scopus 로고
    • Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin
    • Yogesha SD, Sharff A, Bricogne G, Izard T (2011) Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin. Protein Sci 20:1471-1476.
    • (2011) Protein Sci , vol.20 , pp. 1471-1476
    • Yogesha, S.D.1    Sharff, A.2    Bricogne, G.3    Izard, T.4
  • 15
    • 21744441321 scopus 로고    scopus 로고
    • Structural dynamics of α-actinin-vinculin interactions
    • Bois PR, Borgon RA, Vonrhein C, Izard T (2005) Structural dynamics of α-actinin-vinculin interactions. Mol Cell Biol 25:6112-6122.
    • (2005) Mol Cell Biol , vol.25 , pp. 6112-6122
    • Bois, P.R.1    Borgon, R.A.2    Vonrhein, C.3    Izard, T.4
  • 16
  • 17
    • 33750716480 scopus 로고    scopus 로고
    • Shigella applies molecular mimicry to subvert vinculin and invade host cells
    • Izard T, Tran Van Nhieu G, Bois PR (2006) Shigella applies molecular mimicry to subvert vinculin and invade host cells. J Cell Biol 175:465-475.
    • (2006) J Cell Biol , vol.175 , pp. 465-475
    • Izard, T.1    Tran Van Nhieu, G.2    Bois, P.R.3
  • 19
    • 35649016759 scopus 로고    scopus 로고
    • Vinculin binding in its closed conformation by a helix addition mechanism
    • DOI 10.1038/sj.emboj.7601863, PII 7601863
    • Tran Van Nhieu G, Izard T (2007) Vinculin binding in its closed conformation by a helix addition mechanism. Embo J 26:4588-4596. (Pubitemid 350036624)
    • (2007) EMBO Journal , vol.26 , Issue.21 , pp. 4588-4596
    • Tran, V.N.G.1    Izard, T.2
  • 20
    • 80053403384 scopus 로고    scopus 로고
    • The Rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin
    • Park H, Lee JH, Cossart P, Gouin E, Izard T (2011) The Rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin. J Biol Chem 286: 35096-35103.
    • (2011) J Biol Chem , vol.286 , pp. 35096-35103
    • Park, H.1    Lee, J.H.2    Cossart, P.3    Gouin, E.4    Izard, T.5
  • 24
    • 34249705346 scopus 로고    scopus 로고
    • Force-induced activation of Talin and its possible role in focal adhesion mechanotransduction
    • DOI 10.1016/j.jbiomech.2007.04.006, PII S0021929007001649
    • Lee SE, Kamm RD, Mofrad MR (2007) Force-induced activation of talin and its possible role in focal adhesion mechanotransduction. J Biomech 40:2096-2106. (Pubitemid 46843013)
    • (2007) Journal of Biomechanics , vol.40 , Issue.9 , pp. 2096-2106
    • Lee, S.E.1    Kamm, R.D.2    Mofrad, M.R.K.3
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 28
  • 29
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW (1968) Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 30
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Cryst 30: 1022-1025. (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.