메뉴 건너뛰기




Volumn 289, Issue 33, 2014, Pages 23256-23263

The α-subunit regulates stability of the metal ion at the ligand-associated metal ion-binding site in β3 integrins

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; LIGANDS; MOLECULAR DYNAMICS;

EID: 84905977235     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.581470     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • DOI 10.1016/j.ceb.2007.08.002, PII S0955067407001196, Cell to Cell Contact and Extracellular Matrix
    • Arnaout, M. A., Goodman, S. L., and Xiong, J. P. (2007) Structure and mechanics of integrin-based cell adhesion. Curr. Opin. Cell Biol. 19, 495-507 (Pubitemid 350019555)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.-P.3
  • 4
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser, M., Legate, K. R., Zent, R., and Fässler, R. (2009) The tail of integrins, talin, and kindlins. Science 324, 895-899
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fässler, R.4
  • 5
    • 0029664968 scopus 로고    scopus 로고
    • 2+ binding site on the β3-integrins that regulates the dissociation rate for RGD ligands
    • 2+ binding site on the β3-integrins that regulates the dissociation rate for RGD ligands. J. Biol. Chem. 271, 21745-21751
    • (1996) J. Biol. Chem. , vol.271 , pp. 21745-21751
    • Hu, D.D.1    Barbas, C.F.2    Smith, J.W.3
  • 6
    • 0028970566 scopus 로고
    • Regulation of integrin alpha5beta1-fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+
    • DOI 10.1074/jbc.270.44.26270
    • Mould, A. P., Akiyama, S. K., and Humphries, M. J. (1995) Regulation of integrin α5β1-fibronectin interactions by divalent cations: evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+. J. Biol. Chem. 270, 26270-26277 (Pubitemid 3006198)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.44 , pp. 26270-26277
    • Mould, A.P.1    Akiyama, S.K.2    Humphries, M.J.3
  • 8
    • 0025062149 scopus 로고
    • A β3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation
    • Loftus, J. C., O'Toole, T. E., Plow, E. F., Glass, A., Frelinger, A. L., 3rd, and Ginsberg, M. H. (1990) A β3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science 249, 915-918
    • (1990) Science , vol.249 , pp. 915-918
    • Loftus, J.C.1    O'Toole, T.E.2    Plow, E.F.3    Glass, A.4    Frelinger III, A.L.5    Ginsberg, M.H.6
  • 9
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • DOI 10.1126/science.1069040
    • Xiong, J. P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S. L., and Arnaout, M. A. (2002) Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155 (Pubitemid 34280076)
    • (2002) Science , vol.296 , Issue.5565 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 10
    • 44349114473 scopus 로고    scopus 로고
    • Functional and computational studies of the ligand-associated metal binding site of β3 integrins
    • DOI 10.1002/prot.21859
    • Murcia, M., Jirouskova, M., Li, J., Coller, B. S., and Filizola, M. (2008) Functional and computational studies of the ligand-associated metal binding site of β3 integrins. Proteins 71, 1779-1791 (Pubitemid 351732934)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.4 , pp. 1779-1791
    • Murcia, M.1    Jirouskova, M.2    Li, J.3    Coller, B.S.4    Filizola, M.5
  • 11
    • 57749106677 scopus 로고    scopus 로고
    • Distinct roles of β1 metal ion-dependent adhesion site (MIDAS), adjacent to MIDAS (ADMIDAS), and ligand-associated metal-binding site (LIMBS) cationbinding sites in ligand recognition by integrin α2β1
    • Valdramidou, D., Humphries, M. J., and Mould, A. P. (2008) Distinct roles of β1 metal ion-dependent adhesion site (MIDAS), adjacent to MIDAS (ADMIDAS), and ligand-associated metal-binding site (LIMBS) cationbinding sites in ligand recognition by integrin α2β1.J. Biol. Chem. 283, 32704-32714
    • (2008) J. Biol. Chem. , vol.283 , pp. 32704-32714
    • Valdramidou, D.1    Humphries, M.J.2    Mould, A.P.3
  • 12
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu, J., Luo, B. H., Xiao, T., Zhang, C., Nishida, N., and Springer, T. A. (2008) Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol. Cell 32, 849-861
    • (2008) Mol. Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 14
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • DOI 10.1002/1097-0282(2000)56:4<257::AID-BIP10029
    • MacKerell, A. D., Jr., Banavali, N., and Foloppe, N. (2000) Development and current status of the CHARMM force field for nucleic acids. Biopolymers 56, 257-265 (Pubitemid 34105873)
    • (2000) Biopolymers , vol.56 , Issue.4 , pp. 257-265
    • MacKerell Jr., A.D.1    Banavali, N.2    Foloppe, N.3
  • 20
    • 84875974786 scopus 로고    scopus 로고
    • Localized lipid packing of transmembrane domains impedes integrin clustering
    • Mehrbod, M., and Mofrad, M. R. (2013) Localized lipid packing of transmembrane domains impedes integrin clustering. PLoS Comput. Biol. 9, e1002948
    • (2013) PLoS Comput. Biol. , vol.9
    • Mehrbod, M.1    Mofrad, M.R.2
  • 21
    • 84884319266 scopus 로고    scopus 로고
    • On the activation of integrin αIIbß3: Outside-in and inside-out pathways
    • Mehrbod, M., Trisno, S., and Mofrad, M. R. (2013) On the activation of integrin αIIbß3: outside-in and inside-out pathways. Biophys. J. 105, 1304-1315
    • (2013) Biophys. J. , vol.105 , pp. 1304-1315
    • Mehrbod, M.1    Trisno, S.2    Mofrad, M.R.3
  • 23
    • 0035871686 scopus 로고    scopus 로고
    • A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations
    • Kräutler, V., van Gunsteren, W. F., and Hünenberger, P. H. (2001) A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. J. Comput. Chem. 22, 501-508
    • (2001) J. Comput. Chem. , vol.22 , pp. 501-508
    • Kräutler, V.1    Van Gunsteren, W.F.2    Hünenberger, P.H.3
  • 24
    • 0037424598 scopus 로고    scopus 로고
    • Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human αvβ3 integrin
    • DOI 10.1016/S0022-2836(03)00082-2
    • Richards, J., Miller, M., Abend, J., Koide, A., Koide, S., and Dewhurst, S. (2003) Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human αvβ3 integrin. J. Mol. Biol. 326, 1475-1488 (Pubitemid 36269089)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.5 , pp. 1475-1488
    • Richards, J.1    Miller, M.2    Abend, J.3    Koide, A.4    Koide, S.5    Dewhurst, S.6
  • 28
    • 0029780525 scopus 로고    scopus 로고
    • Critical residues of integrin αIIb subunit for binding of αIIbβ3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3)
    • DOI 10.1074/jbc.271.31.18610
    • Kamata, T., Irie, A., Tokuhira, M., and Takada, Y. (1996) Critical residues of integrin αIIb subunit for binding of αIIbß3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J. Biol. Chem. 271, 18610-18615 (Pubitemid 26322724)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.31 , pp. 18610-18615
    • Kamata, T.1    Irie, A.2    Tokuhira, M.3    Takada, Y.4
  • 30
    • 4644272216 scopus 로고    scopus 로고
    • A novel adaptation of the integrin PSI domain revealed from its crystal structure
    • DOI 10.1074/jbc.C400362200
    • Xiong, J. P., Stehle, T., Goodman, S. L., and Arnaout, M. A. (2004) A novel adaptation of the integrin PSI domain revealed from its crystal structure. J. Biol. Chem. 279, 40252-40254 (Pubitemid 39287606)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40252-40254
    • Xiong, J.-P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 31
    • 0026337552 scopus 로고
    • Vitronectin receptor has a role in bone resorption but does not mediate tight sealing zone attachment of osteoclasts to the bone surface
    • Lakkakorpi, P. T., Horton, M. A., Helfrich, M. H., Karhukorpi, E. K., and Väänänen, H. K. (1991) Vitronectin receptor has a role in bone resorption but does not mediate tight sealing zone attachment of osteoclasts to the bone surface. J. Cell Biol. 115, 1179-1186 (Pubitemid 21909964)
    • (1991) Journal of Cell Biology , vol.115 , Issue.4 , pp. 1179-1186
    • Lakkakorpi, P.T.1    Horton, M.A.2    Helfrich, M.H.3    Karhukorpi, E.-K.4    Vaananen, H.K.5
  • 34
    • 21644476221 scopus 로고    scopus 로고
    • Membrane-proximal α/β stalk interactions differentially regulate integrin activation
    • DOI 10.1074/jbc.M409548200
    • Kamata, T., Handa, M., Sato, Y., Ikeda, Y., and Aiso, S. (2005) Membraneproximal α/β stalk interactions differentially regulate integrin activation. J. Biol. Chem. 280, 24775-24783 (Pubitemid 40934568)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24775-24783
    • Kamata, T.1    Handa, M.2    Sato, Y.3    Ikeda, Y.4    Aiso, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.