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Volumn 16, Issue 1, 2008, Pages 72-81

Distinct Structural and Adhesive Roles of Ca2+ in Membrane Binding of Blood Coagulation Factors

Author keywords

CELLBIO; PROTEINS

Indexed keywords

BLOOD CLOTTING FACTOR; BLOOD CLOTTING FACTOR 7A; CALCIUM ION;

EID: 37549054088     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.10.021     Document Type: Article
Times cited : (68)

References (44)
  • 1
    • 2942669901 scopus 로고    scopus 로고
    • The crystal structure of activated protein C-inactivated bovine factor Va: implications for cofactor function
    • Adams T.E., Hockin M.F., Mann K.G., and Everse S.J. The crystal structure of activated protein C-inactivated bovine factor Va: implications for cofactor function. Proc. Natl. Acad. Sci. USA 101 (2004) 8918-8923
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8918-8923
    • Adams, T.E.1    Hockin, M.F.2    Mann, K.G.3    Everse, S.J.4
  • 2
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner D.W., D'Arcy A., Chène C., Winkler F.K., Guha A., Konigsberg W.H., and Nemerson Y. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 380 (1996) 41-46
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chène, C.3    Winkler, F.K.4    Guha, A.5    Konigsberg, W.H.6    Nemerson, Y.7
  • 3
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt T.H., Grinkova Y.V., and Sligar S.G. Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett. 2 (2002) 853-856
    • (2002) Nano Lett. , vol.2 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 4
    • 37549012432 scopus 로고    scopus 로고
    • Big Red. (2007). The Big Red Cluster (http://rac.uits.iu.edu/rats/research/bigred/index.shtml).
  • 6
    • 33846823909 scopus 로고
    • Particle mesh Ewald: an N log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald: an N log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 7
    • 0035968172 scopus 로고    scopus 로고
    • The ω-loop region of the human prothrombin γ-carboxyglutamic acid domain penetrates anionic phospholipid membranes
    • Falls L.A., Furie B.C., Jacobs M., Furie B., and Rigby A.C. The ω-loop region of the human prothrombin γ-carboxyglutamic acid domain penetrates anionic phospholipid membranes. J. Biol. Chem. 276 (2001) 23895-23902
    • (2001) J. Biol. Chem. , vol.276 , pp. 23895-23902
    • Falls, L.A.1    Furie, B.C.2    Jacobs, M.3    Furie, B.4    Rigby, A.C.5
  • 8
    • 0032614136 scopus 로고    scopus 로고
    • Constant surface tension simulations of lipid bilayers: the sensitivity of surface areas and compressibilities
    • Feller S.E., and Pastor R.W. Constant surface tension simulations of lipid bilayers: the sensitivity of surface areas and compressibilities. J. Chem. Phys. 111 (1999) 1281-1287
    • (1999) J. Chem. Phys. , vol.111 , pp. 1281-1287
    • Feller, S.E.1    Pastor, R.W.2
  • 9
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation - the Langevin piston method
    • Feller S.E., Zhang Y.H., Pastor R.W., and Brooks B.R. Constant pressure molecular dynamics simulation - the Langevin piston method. J. Chem. Phys. 103 (1995) 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 10
    • 0030844208 scopus 로고    scopus 로고
    • Molecular dynamics simulation of unsaturated lipid bilayer at low hydration: parameterization and comparison with diffraction studies
    • Feller S.E., Yin D., Pastor R.W., and MacKerell Jr. A.D. Molecular dynamics simulation of unsaturated lipid bilayer at low hydration: parameterization and comparison with diffraction studies. Biophys. J. 73 (1997) 2269-2279
    • (1997) Biophys. J. , vol.73 , pp. 2269-2279
    • Feller, S.E.1    Yin, D.2    Pastor, R.W.3    MacKerell Jr., A.D.4
  • 11
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie B., and Furie B.C. The molecular basis of blood coagulation. Cell 53 (1988) 505-518
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 12
    • 0030707636 scopus 로고    scopus 로고
    • The γ-carboxylation recognition site is sufficient to direct vitamin K-dependent carboxylation on an adjacent glutamate-rich region of thrombin in a propeptide-thrombin chimera
    • Furie B.C., Ratcliffe J.V., Tward J., Jorgensen M.J., Blaszkowsky L.S., DiMichelle D., and Furie B. The γ-carboxylation recognition site is sufficient to direct vitamin K-dependent carboxylation on an adjacent glutamate-rich region of thrombin in a propeptide-thrombin chimera. J. Biol. Chem. 272 (1997) 28258-28262
    • (1997) J. Biol. Chem. , vol.272 , pp. 28258-28262
    • Furie, B.C.1    Ratcliffe, J.V.2    Tward, J.3    Jorgensen, M.J.4    Blaszkowsky, L.S.5    DiMichelle, D.6    Furie, B.7
  • 13
    • 10644281158 scopus 로고    scopus 로고
    • Lysine 5 and phenylalanine 9 of the factor IX ω-loop interact with phosphatidylserine in a membrane-mimetic environment
    • Grant M.A., Baikeev R.F., Gilbert G.E., and Rigby A.C. Lysine 5 and phenylalanine 9 of the factor IX ω-loop interact with phosphatidylserine in a membrane-mimetic environment. Biochemistry 43 (2004) 15367-15378
    • (2004) Biochemistry , vol.43 , pp. 15367-15378
    • Grant, M.A.1    Baikeev, R.F.2    Gilbert, G.E.3    Rigby, A.C.4
  • 14
    • 37549041944 scopus 로고    scopus 로고
    • Grubmüller, H. (1996). Solvate 1.0 (http://www.mpibpc.mpg.de/groups/grubmueller/start/index.html).
  • 15
    • 0001008704 scopus 로고
    • Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal-phases
    • Heller H., Schaefer M., and Schulten K. Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal-phases. J. Phys. Chem. 97 (1993) 8343-8360
    • (1993) J. Phys. Chem. , vol.97 , pp. 8343-8360
    • Heller, H.1    Schaefer, M.2    Schulten, K.3
  • 16
    • 0016774953 scopus 로고
    • Cooperative calcium binding by the phospholipid binding region of bovine prothrombin: a requirement for intact disulfide bridges
    • Henriksen R.A., and Jackson C.M. Cooperative calcium binding by the phospholipid binding region of bovine prothrombin: a requirement for intact disulfide bridges. Arch. Biochem. Biophys. 170 (1975) 149-159
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 149-159
    • Henriksen, R.A.1    Jackson, C.M.2
  • 19
    • 0035312645 scopus 로고    scopus 로고
    • Steered molecular dynamics and mechanical functions of proteins
    • Isralewitz B., Gao M., and Schulten K. Steered molecular dynamics and mechanical functions of proteins. Curr. Opin. Struct. Biol. 11 (2001) 224-230
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 224-230
    • Isralewitz, B.1    Gao, M.2    Schulten, K.3
  • 20
    • 2942750047 scopus 로고    scopus 로고
    • Simulations of a membrane-anchored peptide: structure, dynamics, and influence on bilayer properties
    • Jensen M.Ø., Mouritsen O., and Peters G.H. Simulations of a membrane-anchored peptide: structure, dynamics, and influence on bilayer properties. Biophys. J. 86 (2004) 3556-3575
    • (2004) Biophys. J. , vol.86 , pp. 3556-3575
    • Jensen, M.Ø.1    Mouritsen, O.2    Peters, G.H.3
  • 24
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Martyna G.J., Tobias D.J., and Klein M.L. Constant pressure molecular dynamics algorithms. J. Chem. Phys. 101 (1994) 4177-4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 25
    • 0029903723 scopus 로고    scopus 로고
    • The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor
    • McCallum C.D., Hapak R.C., Neuenschwander P.F., Morrissey J.H., and Johnson A.E. The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor. J. Biol. Chem. 271 (1996) 28168-28175
    • (1996) J. Biol. Chem. , vol.271 , pp. 28168-28175
    • McCallum, C.D.1    Hapak, R.C.2    Neuenschwander, P.F.3    Morrissey, J.H.4    Johnson, A.E.5
  • 26
    • 0030967015 scopus 로고    scopus 로고
    • Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site
    • McDonald J.F., Shah A.M., Schwalbe R.A., Kisiel W., Dahlbäck B., and Nelsestuen G.L. Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site. Biochemistry 36 (1997) 5120-5127
    • (1997) Biochemistry , vol.36 , pp. 5120-5127
    • McDonald, J.F.1    Shah, A.M.2    Schwalbe, R.A.3    Kisiel, W.4    Dahlbäck, B.5    Nelsestuen, G.L.6
  • 27
    • 0035912739 scopus 로고    scopus 로고
    • Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X
    • Mizuno H., Fujimoto Z., Atoda H., and Morita T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc. Natl. Acad. Sci. USA 98 (2001) 7230-7234
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7230-7234
    • Mizuno, H.1    Fujimoto, Z.2    Atoda, H.3    Morita, T.4
  • 29
    • 0032762628 scopus 로고    scopus 로고
    • Enhancement of vitamin-K-dependent protein function by modification of the γ-carboxyglutamic acid domain: studies of protein C and factor VII
    • Nelsestuen G.L. Enhancement of vitamin-K-dependent protein function by modification of the γ-carboxyglutamic acid domain: studies of protein C and factor VII. Trends Cardiovasc. Med. 9 (1999) 162-167
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 162-167
    • Nelsestuen, G.L.1
  • 33
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • Shaw A.W., Pureza V.S., Sligar S.G., and Morrissey J.H. The local phospholipid environment modulates the activation of blood clotting. J. Biol. Chem. 282 (2007) 6556-6563
    • (2007) J. Biol. Chem. , vol.282 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 34
    • 34250372191 scopus 로고    scopus 로고
    • Reparameterization of all-atom dipalmitoylphosphatidylcholine lipid parameters enables simulation of fluid bilayers at zero tension
    • Sonne J., Jensen M.Ø., Hansen F.Y., Hemmingsen L., and Peters G.H. Reparameterization of all-atom dipalmitoylphosphatidylcholine lipid parameters enables simulation of fluid bilayers at zero tension. Biophys. J. 92 (2007) 4157-4167
    • (2007) Biophys. J. , vol.92 , pp. 4157-4167
    • Sonne, J.1    Jensen, M.Ø.2    Hansen, F.Y.3    Hemmingsen, L.4    Peters, G.H.5
  • 35
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor M., and Schulten K. Single-molecule experiments in vitro and in silico. Science 316 (2007) 1144-1148
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 36
    • 33748300590 scopus 로고    scopus 로고
    • Phosphatidic acid- and phosphatidylserine-binding proteins
    • Stace C.L., and Ktistakis N.T. Phosphatidic acid- and phosphatidylserine-binding proteins. Biochim. Biophys. Acta 176 (2006) 913-926
    • (2006) Biochim. Biophys. Acta , vol.176 , pp. 913-926
    • Stace, C.L.1    Ktistakis, N.T.2
  • 38
    • 33846586964 scopus 로고    scopus 로고
    • Computational study of coagulation factor VIIa's affinity for phospholipid membranes
    • Taboureau O., and Olsen O.H. Computational study of coagulation factor VIIa's affinity for phospholipid membranes. Eur. Biophys. J. 36 (2007) 133-144
    • (2007) Eur. Biophys. J. , vol.36 , pp. 133-144
    • Taboureau, O.1    Olsen, O.H.2
  • 39
    • 37549059454 scopus 로고    scopus 로고
    • TeraGrid. (2007). The TeraGrid Portal (http://www.teragrid.org/).
  • 40
    • 0011745370 scopus 로고
    • Molecular dynamics simulation of a bilayer membrane
    • van der Ploeg P., and Berendsen H.J.C. Molecular dynamics simulation of a bilayer membrane. J. Chem. Phys. 76 (1982) 3271-3276
    • (1982) J. Chem. Phys. , vol.76 , pp. 3271-3276
    • van der Ploeg, P.1    Berendsen, H.J.C.2
  • 41
    • 1442285238 scopus 로고    scopus 로고
    • An all-atom solution-equilibrated model for human extrinsic blood coagulation complex (sTF-VIIa-Xa): a protein-protein docking and molecular dynamics refinement study
    • Venkateswarlu D., Duke R., Perera L., Darden T.A., and Pedersen L.G. An all-atom solution-equilibrated model for human extrinsic blood coagulation complex (sTF-VIIa-Xa): a protein-protein docking and molecular dynamics refinement study. J. Thromb. Haemost. 1 (2003) 2577-2588
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2577-2588
    • Venkateswarlu, D.1    Duke, R.2    Perera, L.3    Darden, T.A.4    Pedersen, L.G.5
  • 42
    • 0025324415 scopus 로고
    • γ-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase
    • Vermeer C. γ-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase. Biochem. J. 266 (1990) 625-636
    • (1990) Biochem. J. , vol.266 , pp. 625-636
    • Vermeer, C.1
  • 43
    • 33748747497 scopus 로고    scopus 로고
    • Raising the active site of factor VIIa above the membrane surface reduces its procoagulant activity but not factor VII autoactivation
    • Waters E.K., Yegneswaran S., and Morrissey J.H. Raising the active site of factor VIIa above the membrane surface reduces its procoagulant activity but not factor VII autoactivation. J. Biol. Chem. 281 (2006) 26062-26068
    • (2006) J. Biol. Chem. , vol.281 , pp. 26062-26068
    • Waters, E.K.1    Yegneswaran, S.2    Morrissey, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.