메뉴 건너뛰기




Volumn 65, Issue 2, 2006, Pages 274-279

Unambiguous prediction of human integrin transmembrane heterodimer interactions using only homologous sequences

Author keywords

Homology; Integrins; Membrane; Molecular dynamics; Protein protein interactions

Indexed keywords

ALPHA INTEGRIN; BETA INTEGRIN; GLYCOPHORIN A; INTEGRIN;

EID: 33749038910     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21072     Document Type: Article
Times cited : (14)

References (33)
  • 2
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: Are changes in affinity and conformation underemphasized?
    • Carman CV, Springer TA. Integrin avidity regulation: are changes in affinity and conformation underemphasized? Curr Opin Cell Biol 2003;15:547-556.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 3
    • 0036683057 scopus 로고    scopus 로고
    • Role of integrins in regulating epidermal adhesion, growth and differentiation
    • Watt FM. Role of integrins in regulating epidermal adhesion, growth and differentiation. EMBO J 2002;21:3919-3926.
    • (2002) EMBO J , vol.21 , pp. 3919-3926
    • Watt, F.M.1
  • 4
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M, Carman CV, Springer TA. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003;301:1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 5
    • 0033517796 scopus 로고    scopus 로고
    • Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on αIIbβ3 integrin conformation and oligomerization
    • Hantgan RR, Paumi C, Rocco M, Weisel JW. Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on αIIbβ3 integrin conformation and oligomerization. Biochemistry 1999;38:14461-14474.
    • (1999) Biochemistry , vol.38 , pp. 14461-14474
    • Hantgan, R.R.1    Paumi, C.2    Rocco, M.3    Weisel, J.W.4
  • 7
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin α(IIb)β(3) based on electron cryomicroscopy and X-ray crystallography
    • Adair BD, Yeager M. Three-dimensional model of the human platelet integrin α(IIb)β(3) based on electron cryomicroscopy and X-ray crystallography. Proc Natl Acad Sci USA 2002;99:14059-14064.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 8
    • 14844323604 scopus 로고    scopus 로고
    • Transmembrane domain helix packing stabilizes integrin αIIbβ3 in the low affinity state
    • Partridge AW, Liu S, Kim S, Bowie JU, Ginsberg MH. Transmembrane domain helix packing stabilizes integrin αIIbβ3 in the low affinity state. J Biol Chem 2005;280:7294-7300.
    • (2005) J Biol Chem , vol.280 , pp. 7294-7300
    • Partridge, A.W.1    Liu, S.2    Kim, S.3    Bowie, J.U.4    Ginsberg, M.H.5
  • 9
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo BH, Springer TA, Takagi J. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol 2004;2:e153.
    • (2004) PLoS Biol , vol.2
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 10
    • 18944403970 scopus 로고    scopus 로고
    • A coiled-coil structure of the αIIbβ3 integrin transmembrane and cytoplasmic domains in its resting state
    • Gottschalk KE. A coiled-coil structure of the αIIbβ3 integrin transmembrane and cytoplasmic domains in its resting state. Structure 2005;13:703-712.
    • (2005) Structure , vol.13 , pp. 703-712
    • Gottschalk, K.E.1
  • 12
    • 0037474296 scopus 로고    scopus 로고
    • GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane
    • Schneider D, Engelman DM. GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. J Biol Chem 2003;278:3105-3111.
    • (2003) J Biol Chem , vol.278 , pp. 3105-3111
    • Schneider, D.1    Engelman, D.M.2
  • 13
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by α/β integrins
    • Schneider D, Engelman DM. Involvement of transmembrane domain interactions in signal transduction by α/β integrins. J Biol Chem 2004;279:9840-9846.
    • (2004) J Biol Chem , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.M.2
  • 14
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie KR, Prestegard JH, Engelman DM. A transmembrane helix dimer: structure and implications. Science 1997;276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 16
    • 33645020555 scopus 로고    scopus 로고
    • Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
    • Lin X, Tan SM, Law SKA, Torres J. Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved. Proteins 2006;63:16-23.
    • (2006) Proteins , vol.63 , pp. 16-23
    • Lin, X.1    Tan, S.M.2    Law, S.K.A.3    Torres, J.4
  • 17
    • 0035882546 scopus 로고    scopus 로고
    • A new method to model membrane protein structure based on silent amino acid substitutions
    • Briggs JA, Torres J, Arkin IT. A new method to model membrane protein structure based on silent amino acid substitutions. Proteins 2001;44:370-375.
    • (2001) Proteins , vol.44 , pp. 370-375
    • Briggs, J.A.1    Torres, J.2    Arkin, I.T.3
  • 18
    • 0036111126 scopus 로고    scopus 로고
    • Contribution of energy values to the analysis of global searching molecular dynamics simulations of transmembrane helical bundles
    • Torres J, Briggs JA, Arkin IT. Contribution of energy values to the analysis of global searching molecular dynamics simulations of transmembrane helical bundles. Biophys J 2002;82:3063-3071.
    • (2002) Biophys J , vol.82 , pp. 3063-3071
    • Torres, J.1    Briggs, J.A.2    Arkin, I.T.3
  • 19
    • 0036289317 scopus 로고    scopus 로고
    • Convergence of experimental, computational and evolutionary approaches predicts the presence of a tetrameric form for CD3-ζ
    • Torres J, Briggs JA, Arkin IT. Convergence of experimental, computational and evolutionary approaches predicts the presence of a tetrameric form for CD3-ζ. J Mol Biol 2002;316:375-384.
    • (2002) J Mol Biol , vol.316 , pp. 375-384
    • Torres, J.1    Briggs, J.A.2    Arkin, I.T.3
  • 20
    • 21244448326 scopus 로고    scopus 로고
    • The transmembrane oligomers of coronavirus protein e
    • Torres J, Wang J, Parthasarathy K, Liu DX. The transmembrane oligomers of coronavirus protein E. Biophys J 2005;88:1283-1290.
    • (2005) Biophys J , vol.88 , pp. 1283-1290
    • Torres, J.1    Wang, J.2    Parthasarathy, K.3    Liu, D.X.4
  • 22
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams PD, Arkin IT, Engelman DM, Brunger AT. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nat Struct Biol 1995;2:154-162.
    • (1995) Nat Struct Biol , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 23
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer ELL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001;305:567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 25
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin αIIbβ3 "inside- out" activation as regulated by its cytoplasmic face
    • Vinogradova O, Velyvis A, Velyviene A, Hu B, Haas TA, Plow EF, Qin J. A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face. Cell 2002;110:587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5    Plow, E.F.6    Qin, J.7
  • 26
    • 0037197990 scopus 로고    scopus 로고
    • Solution structures of the cytoplasmic tail complex from platelet integrin αIIb- and β3-subunits
    • Weljie AM, Hwang PM, Vogel HJ. Solution structures of the cytoplasmic tail complex from platelet integrin αIIb- and β3-subunits. Proc Natl Acad Sci USA 2002;99:5878-5883.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5878-5883
    • Weljie, A.M.1    Hwang, P.M.2    Vogel, H.J.3
  • 27
    • 0034652205 scopus 로고    scopus 로고
    • A structural basis for integrin activation by the cytoplasmic tail of the α(IIb)-subunit
    • Vinogradova O, Haas T, Plow EF, Qin J. A structural basis for integrin activation by the cytoplasmic tail of the α(IIb)-subunit. Proc Natl Acad Sci USA 2000;97:1450-1455.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1450-1455
    • Vinogradova, O.1    Haas, T.2    Plow, E.F.3    Qin, J.4
  • 28
    • 0032406838 scopus 로고    scopus 로고
    • Statistical analysis of predicted transmembrane α-helices
    • Arkin IT, Brunger AT. Statistical analysis of predicted transmembrane α-helices. Biochim Biophys Acta 1998;1429:113-128.
    • (1998) Biochim Biophys Acta , vol.1429 , pp. 113-128
    • Arkin, I.T.1    Brunger, A.T.2
  • 29
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions
    • Senes A, Gerstein M, Engelman DM. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions. J Mol Biol 2000;296:921-936.
    • (2000) J Mol Biol , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 30
    • 0037136435 scopus 로고    scopus 로고
    • Genomic analysis of membrane protein families: Abundance and conserved motifs
    • Liu Y, Engelman DM, Gerstein M. Genomic analysis of membrane protein families: abundance and conserved motifs. Genome Biol 2002;3:1-12.
    • (2002) Genome Biol , vol.3 , pp. 1-12
    • Liu, Y.1    Engelman, D.M.2    Gerstein, M.3
  • 31
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002;110:599-611.
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 33
    • 2942587504 scopus 로고    scopus 로고
    • A computational model of transmembrane integrin clustering
    • Gottschalk KE, Kessler H. A computational model of transmembrane integrin clustering. Structure 2004;12:1109-1116.
    • (2004) Structure , vol.12 , pp. 1109-1116
    • Gottschalk, K.E.1    Kessler, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.