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Volumn 21, Issue 4, 2014, Pages 383-388

Structural basis for pure antagonism of integrin α Vβ 3 by a high-affinity form of fibronectin

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; LIGAND; PARTIAL AGONIST; VITRONECTIN RECEPTOR; ALPHA5 BETA3 INTEGRIN INHIBITOR; ARGINYLGLYCYLASPARTIC ACID; BARBOURIN; DISINTEGRIN; EPTIFIBATIDE; FIBRINOGEN RECEPTOR AFFECTING AGENT; MUTANT PROTEIN; PEPTIDOMIMETIC AGENT; PROTEIN INHIBITOR; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84897973151     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2797     Document Type: Article
Times cited : (106)

References (45)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins bidirectional, allosteric signaling machines
    • Hynes, R.O. Integrins: Bidirectional, allosteric signaling machines. Cell 110, 673-687 (2002
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin aVβ3
    • Xiong, J.P. et al. Crystal structure of the extracellular segment of integrin aVβ3. Science 294, 339-345 (2001
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1
  • 3
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout, M.A., Goodman, S.L. & Xiong, J.P. Structure and mechanics of integrin-based cell adhesion. Curr. Opin. Cell Biol. 19, 495-507 (2007
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 4
    • 69449084406 scopus 로고    scopus 로고
    • Crystal structure of the complete integrin aVβ3 ectodomain plus an a/β transmembrane fragment
    • Xiong, J.P. et al. Crystal structure of the complete integrin aVβ3 ectodomain plus an a/β transmembrane fragment. J. Cell Biol. 186, 589-600 (2009
    • (2009) J. Cell Biol , vol.186 , pp. 589-600
    • Xiong, J.P.1
  • 5
    • 0029039630 scopus 로고
    • Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit
    • Honda, S. et al. Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit. J. Biol. Chem. 270, 11947-11954 (1995
    • (1995) J. Biol. Chem , vol.270 , pp. 11947-11954
    • Honda, S.1
  • 6
    • 0026063230 scopus 로고
    • Monoclonal antibodies to ligand-occupied conformers of integrin aIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger, A.L. III, Du, X.P., Plow, E.F. & Ginsberg, M.H. Monoclonal antibodies to ligand-occupied conformers of integrin aIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266, 17106-17111 (1991
    • (1991) J. Biol. Chem , vol.266 , pp. 17106-17111
    • Frelinger III, A.L.1    Du, X.P.2    Plow, E.F.3    Ginsberg, M.H.4
  • 7
    • 79952940482 scopus 로고    scopus 로고
    • Regulation of integrin aIIbβ3 ligand binding and signaling by the metal ion binding sites in the βI domain
    • Raborn, J., Wang, W. & Luo, B.H. Regulation of integrin aIIbβ3 ligand binding and signaling by the metal ion binding sites in the βI domain. Biochemistry 50, 2084-2091 (2011
    • (2011) Biochemistry , vol.50 , pp. 2084-2091
    • Raborn, J.1    Wang, W.2    Luo, B.H.3
  • 8
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls a5β1 function
    • Friedland, J.C., Lee, M.H. & Boettiger, D. Mechanically activated integrin switch controls a5β1 function. Science 323, 642-644 (2009
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 9
    • 77957363101 scopus 로고    scopus 로고
    • Integrins as therapeutic targets: Lessons and opportunities
    • Cox, D., Brennan, M. & Moran, N. Integrins as therapeutic targets: Lessons and opportunities. Nat. Rev. Drug Discov. 9, 804-820 (2010
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 804-820
    • Cox, D.1    Brennan, M.2    Moran, N.3
  • 10
    • 84887408112 scopus 로고    scopus 로고
    • Integrin-modulating therapy prevents fibrosis and autoimmunity in mouse models of scleroderma
    • Gerber, E.E. et al. Integrin-modulating therapy prevents fibrosis and autoimmunity in mouse models of scleroderma. Nature 503, 126-130 (2013
    • (2013) Nature , vol.503 , pp. 126-130
    • Gerber, E.E.1
  • 11
    • 77953073611 scopus 로고    scopus 로고
    • A monoclonal antibody against aVβ3 integrin inhibits development of atherosclerotic lesions in diabetic pigs
    • 18ra11
    • Maile, L.A. et al. A monoclonal antibody against aVβ3 integrin inhibits development of atherosclerotic lesions in diabetic pigs. Sci. Transl. Med. 2, 18ra11 (2010
    • (2010) Sci. Transl. Med , vol.2
    • Maile, L.A.1
  • 12
    • 65849492850 scopus 로고    scopus 로고
    • Drug-induced immune thrombocytopenia: Pathogenesis, diagnosis, and management
    • Aster, R.H., Curtis, B.R., McFarland, J.G. & Bougie, D.W. Drug-induced immune thrombocytopenia: Pathogenesis, diagnosis, and management. J. Thromb. Haemost. 7, 911-918 (2009
    • (2009) J. Thromb. Haemost , vol.7 , pp. 911-918
    • Aster, R.H.1    Curtis, B.R.2    McFarland, J.G.3    Bougie, D.W.4
  • 13
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin aVβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J.P. et al. Crystal structure of the extracellular segment of integrin aVβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155 (2002
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1
  • 14
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao, T., Takagi, J., Coller, B.S., Wang, J.H. & Springer, T.A. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 432, 59-67 (2004
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 15
    • 0347695986 scopus 로고    scopus 로고
    • Role of ADMIDAS cation-binding site in ligand recognition by integrin a5β1
    • Mould, A.P., Barton, S.J., Askari, J.A., Craig, S.E. & Humphries, M.J. Role of ADMIDAS cation-binding site in ligand recognition by integrin a5β1. J. Biol. Chem. 278, 51622-51629 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 51622-51629
    • Mould, A.P.1    Barton, S.J.2    Askari, J.A.3    Craig, S.E.4    Humphries, M.J.5
  • 16
    • 65649101237 scopus 로고    scopus 로고
    • Eptifibatide-induced thrombocytopenia and thrombosis in humans require Fc?RIIa and the integrin β3 cytoplasmic domain
    • Gao, C. et al. Eptifibatide-induced thrombocytopenia and thrombosis in humans require Fc?RIIa and the integrin β3 cytoplasmic domain. J. Clin. Invest. 119, 504-511 (2009
    • (2009) J. Clin. Invest , vol.119 , pp. 504-511
    • Gao, C.1
  • 17
    • 33847032135 scopus 로고    scopus 로고
    • A mechanistic model for paradoxical platelet activation by ligand-mimetic aIIbβ3 (GPIIb/IIIa) antagonists
    • Bassler, N. et al. A mechanistic model for paradoxical platelet activation by ligand-mimetic aIIbβ3 (GPIIb/IIIa) antagonists. Arterioscler. Thromb. Vasc. Biol. 27, e9-e15 (2007
    • (2007) Arterioscler. Thromb. Vasc. Biol , vol.27
    • Bassler, N.1
  • 18
    • 84887212399 scopus 로고    scopus 로고
    • The integrin antagonist cilengitide activates aVβ3, disrupts VE-cadherin localization at cell junctions and enhances permeability in endothelial cells
    • Alghisi, G.C., Ponsonnet, L. & Ruegg, C. The integrin antagonist cilengitide activates aVβ3, disrupts VE-cadherin localization at cell junctions and enhances permeability in endothelial cells. PLoS ONE 4, e4449 (2009
    • (2009) PLoS ONE , vol.4
    • Alghisi, G.C.1    Ponsonnet, L.2    Ruegg, C.3
  • 19
    • 64149106522 scopus 로고    scopus 로고
    • Stimulation of tumor growth and angiogenesis by low concentrations of RGD-mimetic integrin inhibitors
    • Reynolds, A.R. et al. Stimulation of tumor growth and angiogenesis by low concentrations of RGD-mimetic integrin inhibitors. Nat. Med. 15, 392-400 (2009
    • (2009) Nat. Med , vol.15 , pp. 392-400
    • Reynolds, A.R.1
  • 20
    • 84863375270 scopus 로고    scopus 로고
    • Structure-guided design of a high-Affinity platelet integrin aIIbβ3 receptor antagonist that disrupts Mg2+ binding to the MIDAS
    • 125ra132
    • Zhu, J. et al. Structure-guided design of a high-Affinity platelet integrin aIIbβ3 receptor antagonist that disrupts Mg2+ binding to the MIDAS. Sci. Transl. Med. 4, 125ra132 (2012
    • (2012) Sci. Transl. Med , vol.4
    • Zhu, J.1
  • 21
    • 0028245615 scopus 로고
    • Identification of a novel integrin binding site in fibronectin Differential utilization by β3 integrins
    • Bowditch, R.D. et al. Identification of a novel integrin binding site in fibronectin. Differential utilization by β3 integrins. J. Biol. Chem. 269, 10856-10863 (1994
    • (1994) J. Biol. Chem , vol.269 , pp. 10856-10863
    • Bowditch, R.D.1
  • 22
    • 0037424598 scopus 로고    scopus 로고
    • Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human avβ3 integrin
    • Richards, J. et al. Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human avβ3 integrin. J. Mol. Biol. 326, 1475-1488 (2003
    • (2003) J. Mol. Biol , vol.326 , pp. 1475-1488
    • Richards, J.1
  • 23
    • 0032728451 scopus 로고    scopus 로고
    • Development of eptifibatide
    • Scarborough, R.M. Development of eptifibatide. Am. Heart J. 138, 1093-1104 (1999
    • (1999) Am. Heart J. , vol.138 , pp. 1093-1104
    • Scarborough, R.M.1
  • 24
    • 0037205483 scopus 로고    scopus 로고
    • Integrin activation involves a conformational change in the a1 helix of the β subunit A-domain
    • Mould, A.P. et al. Integrin activation involves a conformational change in the a1 helix of the β subunit A-domain. J. Biol. Chem. 277, 19800-19805 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 19800-19805
    • Mould, A.P.1
  • 25
    • 80052187643 scopus 로고    scopus 로고
    • Identification of integrin β subunit mutations that alter affinity for extracellular matrix ligand
    • Kendall, T., Mukai, L., Jannuzi, A.L. & Bunch, T.A. Identification of integrin β subunit mutations that alter affinity for extracellular matrix ligand. J. Biol. Chem. 286, 30981-30993 (2011
    • (2011) J. Biol. Chem , vol.286 , pp. 30981-30993
    • Kendall, T.1    Mukai, L.2    Jannuzi, A.L.3    Bunch, T.A.4
  • 26
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi, J., Petre, B.M., Walz, T. & Springer, T.A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 110, 599-611 (2002
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 27
    • 16844381981 scopus 로고    scopus 로고
    • Three-dimensional EM structure of the ectodomain of integrin aVβ3 in a complex with fibronectin
    • Adair, B.D. et al. Three-dimensional EM structure of the ectodomain of integrin aVβ3 in a complex with fibronectin. J. Cell Biol. 168, 1109-1118 (2005
    • (2005) J. Cell Biol , vol.168 , pp. 1109-1118
    • Adair, B.D.1
  • 28
    • 27544442354 scopus 로고    scopus 로고
    • The mechanisms and dynamics of avβ3 integrin clustering in living cells
    • Cluzel, C. et al. The mechanisms and dynamics of avβ3 integrin clustering in living cells. J. Cell Biol. 171, 383-392 (2005
    • (2005) J. Cell Biol , vol.171 , pp. 383-392
    • Cluzel, C.1
  • 29
    • 0036344265 scopus 로고    scopus 로고
    • Involvement of tumor cell integrin avβ3 in hematogenous metastasis of human melanoma cells
    • Felding-Habermann, B. et al. Involvement of tumor cell integrin avβ3 in hematogenous metastasis of human melanoma cells. Clin. Exp. Metastasis 19, 427-436 (2002
    • (2002) Clin. Exp. Metastasis , vol.19 , pp. 427-436
    • Felding-Habermann, B.1
  • 30
    • 84860273145 scopus 로고    scopus 로고
    • Crystal structure of a5β1 integrin ectodomain: Atomic details of the fibronectin receptor
    • Nagae, M. et al. Crystal structure of a5β1 integrin ectodomain: Atomic details of the fibronectin receptor. J. Cell Biol. 197, 131-140 (2012
    • (2012) J. Cell Biol , vol.197 , pp. 131-140
    • Nagae, M.1
  • 31
    • 66449112293 scopus 로고    scopus 로고
    • An N-glycosylation site on the β-propeller domain of the integrin a5 subunit plays key roles in both its function and site-specific modification by β1,4-N-Acetylglucosaminyltransferase III
    • Sato, Y. et al. An N-glycosylation site on the β-propeller domain of the integrin a5 subunit plays key roles in both its function and site-specific modification by β1,4-N-Acetylglucosaminyltransferase III. J. Biol. Chem. 284, 11873-11881 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 11873-11881
    • Sato, Y.1
  • 32
    • 70349496205 scopus 로고    scopus 로고
    • Clustering of a5β1 integrins determines adhesion strength whereas avβ3 and talin enable mechanotransduction
    • Roca-Cusachs, P., Gauthier, N.C., Del Rio, A. & Sheetz, M.P. Clustering of a5β1 integrins determines adhesion strength whereas avβ3 and talin enable mechanotransduction. Proc. Natl. Acad. Sci. USA 106, 16245-16250 (2009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16245-16250
    • Roca-Cusachs, P.1    Gauthier, N.C.2    Del Rio, A.3    Sheetz, M.P.4
  • 33
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an aI domain, complement receptor type 4
    • Xie, C. et al. Structure of an integrin with an aI domain, complement receptor type 4. EMBO J. 29, 666-679 (2010
    • (2010) EMBO J. , vol.29 , pp. 666-679
    • Xie, C.1
  • 34
  • 35
    • 0005306564 scopus 로고
    • Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor
    • Cheresh, D.A. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc. Natl. Acad. Sci. USA 84, 6471-6475 (1987
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6471-6475
    • Cheresh, D.A.1
  • 36
    • 0032032228 scopus 로고    scopus 로고
    • Transmembrane-Truncated avβ3 integrin retains high affinity for ligand binding: Evidence for an 'inside-out' suppressor?
    • Mehta, R.J. et al. Transmembrane-Truncated avβ3 integrin retains high affinity for ligand binding: Evidence for an 'inside-out' suppressor? Biochem. J. 330, 861-869 (1998
    • (1998) Biochem J. , vol.330 , pp. 861-869
    • Mehta, R.J.1
  • 37
    • 34547106059 scopus 로고    scopus 로고
    • Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins aLβ2 and aIIbβ3
    • Cheng, M. et al. Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins aLβ2 and aIIbβ3. J. Biol. Chem. 282, 18225-18232 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 18225-18232
    • Cheng, M.1
  • 38
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D.J., Aukhil, I. & Erickson, H.P. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164 (1996
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 39
    • 0028984231 scopus 로고
    • An anti-av-integrin antibody that blocks integrin function inhibits the development of a human melanoma in nude mice
    • Mitjans, F. et al. An anti-av-integrin antibody that blocks integrin function inhibits the development of a human melanoma in nude mice. J. Cell Sci. 108, 2825-2838 (1995
    • (1995) J. Cell Sci , vol.108 , pp. 2825-2838
    • Mitjans, F.1
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 43
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 45
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera-A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004.
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


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