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Volumn 46, Issue 11, 2007, Pages 3193-3199

Identification of a basic region on tissue factor that interacts with the first epidermal growth factor-like domain of factor X

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; BIOLOGICAL MEMBRANES; GROWTH KINETICS; MUTAGENESIS; SUBSTRATES;

EID: 33947401039     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi6025193     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg chlorometheylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode, W., Mayr, I., Baumann, U., Huber, R., Stone, S. R., and Hofsteenge, J. (1989) The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg chlorometheylketone and significance of the Tyr-Pro-Pro-Trp insertion segment, EMBO J. 8, 3467-3475.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 4
    • 0023643043 scopus 로고
    • Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initiation of the coagulation protease cascade
    • Morrissey, J. H., Fakhrai, H., and Edgington, T. S. (1987) Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initiation of the coagulation protease cascade, Cell 50, 129-135.
    • (1987) Cell , vol.50 , pp. 129-135
    • Morrissey, J.H.1    Fakhrai, H.2    Edgington, T.S.3
  • 6
    • 0028094639 scopus 로고
    • Structure of the extracellular domain of human tissue factor: Location of the factor VIIa binding site
    • Muller, Y. A., Ultsch, M. H., Kelley, R. F., and de Vos, A. M. (1994) Structure of the extracellular domain of human tissue factor: Location of the factor VIIa binding site, Biochemistry 33, 10864-10870.
    • (1994) Biochemistry , vol.33 , pp. 10864-10870
    • Muller, Y.A.1    Ultsch, M.H.2    Kelley, R.F.3    de Vos, A.M.4
  • 7
    • 0028299054 scopus 로고
    • Mutational mapping of functional residues in tissue factor: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
    • Ruf, W., Schullek, J. R., Stone, M. J., and Edgington, T. S. (1994) Mutational mapping of functional residues in tissue factor: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain, Biochemistry 33, 1565-1572.
    • (1994) Biochemistry , vol.33 , pp. 1565-1572
    • Ruf, W.1    Schullek, J.R.2    Stone, M.J.3    Edgington, T.S.4
  • 8
    • 0029978704 scopus 로고    scopus 로고
    • Tissue factor residue Asp44 regulates catalytic function of the bound proteinase factor VIIa
    • Kelly, C. R., Schullek, J. R., Ruf, W., and Edgington, T. S. (1996) Tissue factor residue Asp44 regulates catalytic function of the bound proteinase factor VIIa, Biochem. J. 315, 145-151.
    • (1996) Biochem. J , vol.315 , pp. 145-151
    • Kelly, C.R.1    Schullek, J.R.2    Ruf, W.3    Edgington, T.S.4
  • 9
    • 0027022713 scopus 로고
    • Expression and purification of a soluble tissue factor fusion protein with an epitope for an unusual calcium-dependent antibody
    • Rezaie, A. R., Fiore, M. M., Neuenschwander, P. F., Esmon, C. T., and Morrissey, J. H. (1992) Expression and purification of a soluble tissue factor fusion protein with an epitope for an unusual calcium-dependent antibody, Protein Expression Purif. 3, 453-460.
    • (1992) Protein Expression Purif , vol.3 , pp. 453-460
    • Rezaie, A.R.1    Fiore, M.M.2    Neuenschwander, P.F.3    Esmon, C.T.4    Morrissey, J.H.5
  • 10
    • 0034720739 scopus 로고    scopus 로고
    • The tissue factor region that interacts with substrates factor IX and factor X
    • Kirchofer, D., Lipari, M. T., Moran, P., Eigenbrot, C., and Kelley, R. F. (2000) The tissue factor region that interacts with substrates factor IX and factor X, Biochemistry 39, 7380-7387.
    • (2000) Biochemistry , vol.39 , pp. 7380-7387
    • Kirchofer, D.1    Lipari, M.T.2    Moran, P.3    Eigenbrot, C.4    Kelley, R.F.5
  • 11
    • 0017660808 scopus 로고
    • Kinetics of the activation of bovine coagulation factor X by components of the extrinsic pathway. Kinetic behavior of two-chin factor VII in the presence and absence of tissue factor
    • Silverberg, S. A., Nemerson, Y., and Zur, M. (1977) Kinetics of the activation of bovine coagulation factor X by components of the extrinsic pathway. Kinetic behavior of two-chin factor VII in the presence and absence of tissue factor, J. Biol. Chem. 252, 8481-8488.
    • (1977) J. Biol. Chem , vol.252 , pp. 8481-8488
    • Silverberg, S.A.1    Nemerson, Y.2    Zur, M.3
  • 13
    • 0030778627 scopus 로고    scopus 로고
    • Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain
    • McCallum, C. D., Su, B., Neuenschwander, P. F., Morrissey, J. H., and Johnson, A. E. (1997) Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain, J. Biol. Chem. 272, 30160-30166.
    • (1997) J. Biol. Chem , vol.272 , pp. 30160-30166
    • McCallum, C.D.1    Su, B.2    Neuenschwander, P.F.3    Morrissey, J.H.4    Johnson, A.E.5
  • 14
    • 0242362193 scopus 로고    scopus 로고
    • The tissue factor/factor VIIa/factor Xa complex: A model built by docking and site-directed mutagenesis
    • Norledge, B. V., Petrovan, R. J., Ruf, W., and Olson, A. J. (2003) The tissue factor/factor VIIa/factor Xa complex: A model built by docking and site-directed mutagenesis, Proteins 53, 640-648.
    • (2003) Proteins , vol.53 , pp. 640-648
    • Norledge, B.V.1    Petrovan, R.J.2    Ruf, W.3    Olson, A.J.4
  • 15
    • 1442285238 scopus 로고    scopus 로고
    • An all-atom solution-equilibrated model of human extrinsic blood coagulation complex (sTF-VIIa-Xa): A protein-protein docking and molecular dynamics refinement study
    • Venkateswarlu, D., Duke, R. E., Perera, L., Darden, T. A., and Pedersen, L. G. (2003) An all-atom solution-equilibrated model of human extrinsic blood coagulation complex (sTF-VIIa-Xa): A protein-protein docking and molecular dynamics refinement study, J. Thromb. Haemostasis 1, 2577-2588.
    • (2003) J. Thromb. Haemostasis , vol.1 , pp. 2577-2588
    • Venkateswarlu, D.1    Duke, R.E.2    Perera, L.3    Darden, T.A.4    Pedersen, L.G.5
  • 16
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie, B., and Furie, B. C. (1988) The molecular basis of blood coagulation, Cell 53, 505-518.
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 17
    • 0026063331 scopus 로고
    • Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors
    • Stenflo, J. (1991) Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors, Blood 78, 1637-1651.
    • (1991) Blood , vol.78 , pp. 1637-1651
    • Stenflo, J.1
  • 18
    • 0029992658 scopus 로고    scopus 로고
    • Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa
    • Dickinson, C. D., Kelly, C. R., and Ruf, W. (1996) Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa, Proc. Natl. Acad. Sci. U.S.A. 93, 14379-14384.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 14379-14384
    • Dickinson, C.D.1    Kelly, C.R.2    Ruf, W.3
  • 19
    • 0026733665 scopus 로고
    • Cofactor residues lysine 165 and 166 are critical for protein substrate recognition by the tissue factor-factor VIIa protease complex
    • Ruf, W., Miles, D. J., Rehemtulla, A., and Edgington, T. S. (1992) Cofactor residues lysine 165 and 166 are critical for protein substrate recognition by the tissue factor-factor VIIa protease complex, J. Biol. Chem. 267, 6375-6381.
    • (1992) J. Biol. Chem , vol.267 , pp. 6375-6381
    • Ruf, W.1    Miles, D.J.2    Rehemtulla, A.3    Edgington, T.S.4
  • 21
    • 0036479111 scopus 로고    scopus 로고
    • The N-terminal epidermal growth factor-like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor
    • Zhong, D., Bajaj, M. S., Schmidt, A. E., and Bajaj, S. P. (2002) The N-terminal epidermal growth factor-like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor, J. Biol. Chem. 277, 3622-3631.
    • (2002) J. Biol. Chem , vol.277 , pp. 3622-3631
    • Zhong, D.1    Bajaj, M.S.2    Schmidt, A.E.3    Bajaj, S.P.4
  • 22
    • 4544282981 scopus 로고    scopus 로고
    • The cofactor function of the N-terminal domain of tissue factor
    • Kittur, F. S., Manithody, C., Morrissey, J. H., and Rezaie, A. R. (2004) The cofactor function of the N-terminal domain of tissue factor, J. Biol. Chem. 279, 39745-39749.
    • (2004) J. Biol. Chem , vol.279 , pp. 39745-39749
    • Kittur, F.S.1    Manithody, C.2    Morrissey, J.H.3    Rezaie, A.R.4
  • 23
    • 25444475057 scopus 로고    scopus 로고
    • Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor
    • Rezaie, A. R., Manithody, C., and Yang, L. (2005) Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor, J. Biol. Chem. 280, 32722-32728.
    • (2005) J. Biol. Chem , vol.280 , pp. 32722-32728
    • Rezaie, A.R.1    Manithody, C.2    Yang, L.3
  • 24
    • 0027401996 scopus 로고
    • Analysis of the functions of the first epidermal growth factor-like domain of factor X
    • Rezaie, A. R., Neuenschwander, P. F., Morrissey, J. H., and Esmon, C. T. (1993) Analysis of the functions of the first epidermal growth factor-like domain of factor X, J. Biol. Chem. 268, 8176-8180.
    • (1993) J. Biol. Chem , vol.268 , pp. 8176-8180
    • Rezaie, A.R.1    Neuenschwander, P.F.2    Morrissey, J.H.3    Esmon, C.T.4
  • 25
    • 0037076527 scopus 로고    scopus 로고
    • Contribution of basic residues of the 70-80-loop to heparin binding and anticoagulant function of activated protein C
    • Yang, L., Manithody, C., and Rezaie, A. R. (2002) Contribution of basic residues of the 70-80-loop to heparin binding and anticoagulant function of activated protein C, Biochemistry 41, 6149-6157.
    • (2002) Biochemistry , vol.41 , pp. 6149-6157
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 26
    • 0027972573 scopus 로고
    • Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C
    • Smirnov, M. D., and Esmon, C. T. (1994) Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C, J. Biol. Chem. 269, 816-819.
    • (1994) J. Biol. Chem , vol.269 , pp. 816-819
    • Smirnov, M.D.1    Esmon, C.T.2
  • 27
    • 9144240494 scopus 로고    scopus 로고
    • + and factor Va in the prothrombinase complex
    • + and factor Va in the prothrombinase complex, J. Biol. Chem. 279, 48262-48269.
    • (2004) J. Biol. Chem , vol.279 , pp. 48262-48269
    • Rezaie, A.R.1    Kittur, F.S.2
  • 28
    • 0033588095 scopus 로고    scopus 로고
    • Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking
    • Shobe, J., Dickinson, C. D., Edgington, T. S., and Ruf, W. (1999) Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking, J. Biol. Chem. 274, 24171-24175.
    • (1999) J. Biol. Chem , vol.274 , pp. 24171-24175
    • Shobe, J.1    Dickinson, C.D.2    Edgington, T.S.3    Ruf, W.4
  • 29
    • 0034665994 scopus 로고    scopus 로고
    • Exosite Interactions determine the affinity of factor X for the extrinsic Xase complex
    • Baugh, R. J., Dickinson, C. D., Ruf, W., and Krishnaswamy, S. (2000) Exosite Interactions determine the affinity of factor X for the extrinsic Xase complex, J. Biol. Chem. 275, 28826-28833.
    • (2000) J. Biol. Chem , vol.275 , pp. 28826-28833
    • Baugh, R.J.1    Dickinson, C.D.2    Ruf, W.3    Krishnaswamy, S.4
  • 30
    • 0026540132 scopus 로고
    • Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and factor VII
    • Ruf, W., Miles, D. J., Rehemtulla, A., and Edgington, T. S. (1992) Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and factor VII, J. Biol. Chem. 267, 22206-22210.
    • (1992) J. Biol. Chem , vol.267 , pp. 22206-22210
    • Ruf, W.1    Miles, D.J.2    Rehemtulla, A.3    Edgington, T.S.4
  • 31
    • 0026630971 scopus 로고
    • Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding
    • Ullner, M., Selander, M., Persson, E., Stenflo, J., Drakenberg, T., and Teleman, O. (1992) Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding, Biochemistry 31, 5974-5983.
    • (1992) Biochemistry , vol.31 , pp. 5974-5983
    • Ullner, M.1    Selander, M.2    Persson, E.3    Stenflo, J.4    Drakenberg, T.5    Teleman, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.