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Volumn 7, Issue 11, 2012, Pages

Modeling and Molecular Dynamics of HPA-1a and -1b Polymorphisms: Effects on the Structure of the β3 Subunit of the αIIbβ3 Integrin

Author keywords

[No Author keywords available]

Indexed keywords

BETA3 INTEGRIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR 1; EPIDERMAL GROWTH FACTOR 2; LEUCINE; PROLINE; THROMBOCYTE ANTIGEN; THROMBOCYTE ANTIGEN 1A; THROMBOCYTE ANTIGEN 1B; UNCLASSIFIED DRUG;

EID: 84869121086     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047304     Document Type: Article
Times cited : (36)

References (52)
  • 1
    • 85083136989 scopus 로고    scopus 로고
    • Platelets
    • Michelson AD, editors, London: Academic Press
    • Kaplan C, Freedman J (2007) Platelets. In: Michelson AD, editors. Platelets. London: Academic Press. 971-984.
    • (2007) Platelets , pp. 971-984
    • Kaplan, C.1    Freedman, J.2
  • 2
    • 84869139876 scopus 로고    scopus 로고
    • Neonatal alloimmune thrombocytopenia
    • McCrae KR, editors, Taylor & Francis Group
    • Kaplan C (2006) Neonatal alloimmune thrombocytopenia. In: McCrae KR, editors. Thrombocytopenia. Taylor & Francis Group. 223-244.
    • (2006) Thrombocytopenia , pp. 223-244
    • Kaplan, C.1
  • 3
    • 0029875770 scopus 로고    scopus 로고
    • A polymorphism of a platelet glycoprotein receptor as an inherited risk factor for coronary thrombosis
    • Weiss EJ, Bray PF, Tayback M, Schulman SP, Kickler TS, et al. (1996) A polymorphism of a platelet glycoprotein receptor as an inherited risk factor for coronary thrombosis. N Engl J Med 334: 1090-1094.
    • (1996) N Engl J Med , vol.334 , pp. 1090-1094
    • Weiss, E.J.1    Bray, P.F.2    Tayback, M.3    Schulman, S.P.4    Kickler, T.S.5
  • 4
    • 0024588794 scopus 로고
    • The human platelet alloantigens, PlA1 and PlA2, are associated with a leucine33/proline33 amino acid polymorphism in membrane glycoprotein IIIa, and are distinguishable by DNA typing
    • Newman PJ, Derbes RS, Aster RH, (1989) The human platelet alloantigens, PlA1 and PlA2, are associated with a leucine33/proline33 amino acid polymorphism in membrane glycoprotein IIIa, and are distinguishable by DNA typing. J Clin Invest 83: 1778-1781.
    • (1989) J Clin Invest , vol.83 , pp. 1778-1781
    • Newman, P.J.1    Derbes, R.S.2    Aster, R.H.3
  • 5
    • 0029018097 scopus 로고
    • Involvement of the cystein-rich domain of glycoprotein IIIa in the expression of the human platelet alloantigen, PlA1: Evidence for heterogeneity in the humoral response
    • Valentin N, Visentin GP, Newman PJ, (1995) Involvement of the cystein-rich domain of glycoprotein IIIa in the expression of the human platelet alloantigen, PlA1: Evidence for heterogeneity in the humoral response. Blood 85: 3028-3033.
    • (1995) Blood , vol.85 , pp. 3028-3033
    • Valentin, N.1    Visentin, G.P.2    Newman, P.J.3
  • 6
    • 0029858233 scopus 로고    scopus 로고
    • Inhibition of binding of anti-PlA1 antibodies to platelets with monoclonal antibody LK-4, evidence for multiple PlA1 receptor sites on platelet GP IIIa
    • Liu LX, Nardi M, Casella JF, Karpatkin S, (1996) Inhibition of binding of anti-PlA1 antibodies to platelets with monoclonal antibody LK-4, evidence for multiple PlA1 receptor sites on platelet GP IIIa. Blood 88: 3601-3607.
    • (1996) Blood , vol.88 , pp. 3601-3607
    • Liu, L.X.1    Nardi, M.2    Casella, J.F.3    Karpatkin, S.4
  • 7
    • 0026614360 scopus 로고
    • Leucine33-proline33 substitution in human platelet glycoprotein IIIa determines HLA-DRw52a (Dw24) association of the immune response against HPA-1a (Zwa/PlA1) and HPA-1b (Zwb/PlA2)
    • Kuijpers RW, von dem Borne AE, Kiefel V, Mueller-Eckhardt CM, Waters AH, et al. (1992) Leucine33-proline33 substitution in human platelet glycoprotein IIIa determines HLA-DRw52a (Dw24) association of the immune response against HPA-1a (Zwa/PlA1) and HPA-1b (Zwb/PlA2). Hum Immunol 34: 253-256.
    • (1992) Hum Immunol , vol.34 , pp. 253-256
    • Kuijpers, R.W.1    von dem Borne, A.E.2    Kiefel, V.3    Mueller-Eckhardt, C.M.4    Waters, A.H.5
  • 8
    • 0037687696 scopus 로고    scopus 로고
    • A meta-analysis of studies on the association of the platelet PlA polymorphism of glycoprotein IIIa and risk of coronary heart disease
    • Burr D, Doss H, Cooke GE, Goldschmidt-Clermont PJ, (2003) A meta-analysis of studies on the association of the platelet PlA polymorphism of glycoprotein IIIa and risk of coronary heart disease. Stat Med 22: 1741-1760.
    • (2003) Stat Med , vol.22 , pp. 1741-1760
    • Burr, D.1    Doss, H.2    Cooke, G.E.3    Goldschmidt-Clermont, P.J.4
  • 9
    • 0035071454 scopus 로고    scopus 로고
    • Platelet glycoprotein receptor IIIa polymorphism PLA1/PLA2 and coronary risk: a meta-analysis
    • Di Castelnuovo A, de Gaetano G, Donati MB, Iacoviello L, (2001) Platelet glycoprotein receptor IIIa polymorphism PLA1/PLA2 and coronary risk: a meta-analysis. Thromb Haemost 85: 626-633.
    • (2001) Thromb Haemost , vol.85 , pp. 626-633
    • Di Castelnuovo, A.1    de Gaetano, G.2    Donati, M.B.3    Iacoviello, L.4
  • 10
    • 33744976086 scopus 로고    scopus 로고
    • Molecular mechanisms of prothrombotic risk due to genetic variations in platelet genes: Enhanced outside-in signaling through the Pro33 variant of integrin beta3
    • Vijayan KV, Bray PF, (2006) Molecular mechanisms of prothrombotic risk due to genetic variations in platelet genes: Enhanced outside-in signaling through the Pro33 variant of integrin beta3. Exp Biol Med (Maywood) 231: 505-513.
    • (2006) Exp Biol Med (Maywood) , vol.231 , pp. 505-513
    • Vijayan, K.V.1    Bray, P.F.2
  • 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 BH, Xiao T, Zhang C, Nishida N, et al. (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
  • 13
    • 0034669774 scopus 로고    scopus 로고
    • Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks
    • de Brevern AG, Etchebest C, Hazout S, (2000) Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks. Proteins 41: 271-287.
    • (2000) Proteins , vol.41 , pp. 271-287
    • de Brevern, A.G.1    Etchebest, C.2    Hazout, S.3
  • 14
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 15
    • 69449084406 scopus 로고    scopus 로고
    • Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment
    • Xiong JP, Mahalingham B, Alonso JL, Borrelli LA, Rui X, et al. (2009) Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment. J Cell Biol 186: 589-600.
    • (2009) J Cell Biol , vol.186 , pp. 589-600
    • Xiong, J.P.1    Mahalingham, B.2    Alonso, J.L.3    Borrelli, L.A.4    Rui, X.5
  • 17
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 18
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS All-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J, (1996) Development and testing of the OPLS All-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 118: 11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 20
    • 84986440341 scopus 로고
    • SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto S, Kollman PA, (1992) SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models. J Comput Chem 13: 952-962.
    • (1992) J Comput Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 22
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N. log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An N. log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 24
    • 41149083129 scopus 로고    scopus 로고
    • Protein contacts, inter-residue interactions and side-chain modelling
    • Faure G, Bornot A, de Brevern AG, (2008) Protein contacts, inter-residue interactions and side-chain modelling. Biochimie 90: 626-639.
    • (2008) Biochimie , vol.90 , pp. 626-639
    • Faure, G.1    Bornot, A.2    de Brevern, A.G.3
  • 25
    • 2942522721 scopus 로고    scopus 로고
    • ASAView: database and tool for solvent accessibility representation in proteins
    • Ahmad S, Gromiha M, Fawareh H, Sarai A, (2004) ASAView: database and tool for solvent accessibility representation in proteins. BMC Bioinformatics 5: 51.
    • (2004) BMC Bioinformatics , vol.5 , pp. 51
    • Ahmad, S.1    Gromiha, M.2    Fawareh, H.3    Sarai, A.4
  • 28
    • 84864278553 scopus 로고    scopus 로고
    • Progressive structure-based alignment of homologous proteins: Adopting sequence comparison strategies
    • Joseph AP, Srinivasan N, de Brevern AG (2012) Progressive structure-based alignment of homologous proteins: Adopting sequence comparison strategies. Biochimie in press.
    • (2012) Biochimie
    • Joseph, A.P.1    Srinivasan, N.2    de Brevern, A.G.3
  • 29
    • 23144464778 scopus 로고    scopus 로고
    • A structural model of a seven-transmembrane helix receptor: the Duffy antigen/receptor for chemokine (DARC)
    • de Brevern AG, Wong H, Tournamille C, Colin Y, Le Van KC, et al. (2005) A structural model of a seven-transmembrane helix receptor: the Duffy antigen/receptor for chemokine (DARC). Biochim Biophys Acta 1724: 288-306.
    • (2005) Biochim Biophys Acta , vol.1724 , pp. 288-306
    • de Brevern, A.G.1    Wong, H.2    Tournamille, C.3    Colin, Y.4    Le van, K.C.5
  • 30
    • 68949178663 scopus 로고    scopus 로고
    • Protein short loop prediction in terms of a structural alphabet
    • Tyagi M, Bornot A, Offmann B, de Brevern AG, (2009) Protein short loop prediction in terms of a structural alphabet. Comput Biol Chem 33: 329-333.
    • (2009) Comput Biol Chem , vol.33 , pp. 329-333
    • Tyagi, M.1    Bornot, A.2    Offmann, B.3    de Brevern, A.G.4
  • 31
    • 23144437382 scopus 로고    scopus 로고
    • New assessment of a structural alphabet
    • de Brevern AG, (2005) New assessment of a structural alphabet. In Silico Biol 5: 283-289.
    • (2005) In Silico Biol , vol.5 , pp. 283-289
    • de Brevern, A.G.1
  • 32
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao T, Takagi J, Coller BS, Wang JH, Springer TA, (2004) Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 432: 59-67.
    • (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
  • 33
    • 77149172820 scopus 로고    scopus 로고
    • AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function
    • Jallu V, Dusseaux M, Panzer S, Torchet MF, Hezard N, et al. (2010) AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function. Hum Mutat 31: 237-246.
    • (2010) Hum Mutat , vol.31 , pp. 237-246
    • Jallu, V.1    Dusseaux, M.2    Panzer, S.3    Torchet, M.F.4    Hezard, N.5
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF, (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • Macarthur MW, Thornton JM, (1991) Influence of proline residues on protein conformation. J Mol Biol 218: 397-412.
    • (1991) J Mol Biol , vol.218 , pp. 397-412
    • Macarthur, M.W.1    Thornton, J.M.2
  • 36
    • 0025351555 scopus 로고
    • Epitopes on protein antigens: misconceptions and realities
    • Laver WG, Air GM, Webster RG, Smith-Gill SJ, (1990) Epitopes on protein antigens: misconceptions and realities. Cell 61: 553-556.
    • (1990) Cell , vol.61 , pp. 553-556
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3    Smith-Gill, S.J.4
  • 37
    • 78650628653 scopus 로고    scopus 로고
    • A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures
    • Lollier V, Denery-Papini S, Larre C, Tessier D, (2011) A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures. Mol Immunol 48: 577-585.
    • (2011) Mol Immunol , vol.48 , pp. 577-585
    • Lollier, V.1    Denery-Papini, S.2    Larre, C.3    Tessier, D.4
  • 39
    • 79551716021 scopus 로고    scopus 로고
    • Prediction of discontinuous B-cell epitopes using logistic regression and structural information
    • Liu R, Hu J, (2011) Prediction of discontinuous B-cell epitopes using logistic regression and structural information. Proteomics Bioinform 4: 10-15.
    • (2011) Proteomics Bioinform , vol.4 , pp. 10-15
    • Liu, R.1    Hu, J.2
  • 41
    • 0031112230 scopus 로고    scopus 로고
    • An integrin polymorphism that defines reactivity with alloantibodies generates an anchor for MHC class II peptide binding: a model for unidirectional alloimmune responses
    • Wu S, Maslanka K, Gorski J, (1997) An integrin polymorphism that defines reactivity with alloantibodies generates an anchor for MHC class II peptide binding: a model for unidirectional alloimmune responses. J Immunol 158: 3221-3226.
    • (1997) J Immunol , vol.158 , pp. 3221-3226
    • Wu, S.1    Maslanka, K.2    Gorski, J.3
  • 42
    • 70349235983 scopus 로고    scopus 로고
    • Naturally processed peptides spanning the HPA-1a polymorphism are efficiently generated and displayed from platelet glycoprotein by HLA-DRB3*0101-positive antigen-presenting cells
    • Anani Sarab G, Moss M, Barker RN, Urbaniak SJ, (2009) Naturally processed peptides spanning the HPA-1a polymorphism are efficiently generated and displayed from platelet glycoprotein by HLA-DRB3*0101-positive antigen-presenting cells. Blood 114: 1954-1957.
    • (2009) Blood , vol.114 , pp. 1954-1957
    • Anani Sarab, G.1    Moss, M.2    Barker, R.N.3    Urbaniak, S.J.4
  • 43
    • 0033134767 scopus 로고    scopus 로고
    • Construction of a human platelet alloantigen-1a epitope(s) within murine glycoprotein IIIa: identification of residues critical to the conformation of the antibody binding site(s)
    • Barron-Casella EA, Nebbia G, Rogers OC, King KE, Kickler TS, et al. (1999) Construction of a human platelet alloantigen-1a epitope(s) within murine glycoprotein IIIa: identification of residues critical to the conformation of the antibody binding site(s). Blood 93: 2959-2967.
    • (1999) Blood , vol.93 , pp. 2959-2967
    • Barron-Casella, E.A.1    Nebbia, G.2    Rogers, O.C.3    King, K.E.4    Kickler, T.S.5
  • 44
    • 38349186177 scopus 로고    scopus 로고
    • Immunologic and structural analysis of eight novel domain-deletion beta3 integrin peptides designed for detection of HPA-1 antibodies
    • Stafford P, Ghevaert C, Campbell K, Proulx C, Smith G, et al. (2008) Immunologic and structural analysis of eight novel domain-deletion beta3 integrin peptides designed for detection of HPA-1 antibodies. J Thromb Haemost 6: 366-375.
    • (2008) J Thromb Haemost , vol.6 , pp. 366-375
    • Stafford, P.1    Ghevaert, C.2    Campbell, K.3    Proulx, C.4    Smith, G.5
  • 45
    • 33646260186 scopus 로고    scopus 로고
    • A naturally occurring LeuVal mutation in beta3-integrin impairs the HPA-1a epitope: the third allele of HPA-1
    • Santoso S, Kroll H, Andrei-Selmer CL, Socher I, Rankin A, et al. (2006) A naturally occurring LeuVal mutation in beta3-integrin impairs the HPA-1a epitope: the third allele of HPA-1. Transfusion 46: 790-799.
    • (2006) Transfusion , vol.46 , pp. 790-799
    • Santoso, S.1    Kroll, H.2    Andrei-Selmer, C.L.3    Socher, I.4    Rankin, A.5
  • 46
    • 0034071311 scopus 로고    scopus 로고
    • The Pl(A2) allele and cardiovascular disease: the pro(33) and con
    • Byzova TV, Plow EF, (2000) The Pl(A2) allele and cardiovascular disease: the pro(33) and con. J Clin Invest 105: 697-698.
    • (2000) J Clin Invest , vol.105 , pp. 697-698
    • Byzova, T.V.1    Plow, E.F.2
  • 47
    • 0035872215 scopus 로고    scopus 로고
    • Effect of the PlA2 alloantigen on the function of β3-integrins in platelets
    • Bennett JS, Catella-Lawson F, Rut AR, Vilaire G, Qi W, et al. (2001) Effect of the PlA2 alloantigen on the function of β3-integrins in platelets. Blood 97: 3093-3099.
    • (2001) Blood , vol.97 , pp. 3093-3099
    • Bennett, J.S.1    Catella-Lawson, F.2    Rut, A.R.3    Vilaire, G.4    Qi, W.5
  • 48
    • 0034073762 scopus 로고    scopus 로고
    • The Pl(A2) polymorphism of integrin beta(3) enhances outside-in signaling and adhesive functions
    • Vijayan KV, Goldschmidt-Clermont PJ, Roos C, Bray PF, (2000) The Pl(A2) polymorphism of integrin beta(3) enhances outside-in signaling and adhesive functions. J Clin Invest 105: 793-802.
    • (2000) J Clin Invest , vol.105 , pp. 793-802
    • Vijayan, K.V.1    Goldschmidt-Clermont, P.J.2    Roos, C.3    Bray, P.F.4
  • 49
    • 33847680431 scopus 로고    scopus 로고
    • HPA-1 polymorphism of alphaIIbbeta3 modulates platelet adhesion onto immobilized fibrinogen in an in-vitro flow system
    • Loncar R, Stoldt V, Hellmig S, Zotz RB, Mihalj M, et al. (2007) HPA-1 polymorphism of alphaIIbbeta3 modulates platelet adhesion onto immobilized fibrinogen in an in-vitro flow system. Thromb J 5: 1.
    • (2007) Thromb J , vol.5 , pp. 1
    • Loncar, R.1    Stoldt, V.2    Hellmig, S.3    Zotz, R.B.4    Mihalj, M.5
  • 51
    • 0025910094 scopus 로고
    • Selective recognition of adhesive sites in surface-bound fibrinogen by glycoprotein IIb-IIIa on non-activated platelets
    • Savage B, Ruggeri ZM, (1991) Selective recognition of adhesive sites in surface-bound fibrinogen by glycoprotein IIb-IIIa on non-activated platelets. J Biol Chem 266: 11227-11233.
    • (1991) J Biol Chem , vol.266 , pp. 11227-11233
    • Savage, B.1    Ruggeri, Z.M.2
  • 52
    • 82455189778 scopus 로고    scopus 로고
    • Regulation of integrin affinity on cell surfaces
    • Schurpf T, Springer TA, (2011) Regulation of integrin affinity on cell surfaces. EMBO J 30: 4712-4727.
    • (2011) EMBO J , vol.30 , pp. 4712-4727
    • Schurpf, T.1    Springer, T.A.2


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