메뉴 건너뛰기




Volumn 43, Issue 18, 2004, Pages 5246-5255

Allosteric Changes in Solvent Accessibility Observed in Thrombin upon Active Site Occupation

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; KETONES; NEGATIVE IONS; PROTEINS;

EID: 2442419061     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0499718     Document Type: Article
Times cited : (37)

References (32)
  • 1
    • 2442458906 scopus 로고
    • CRC Press, Boca Raton, FL
    • Machovich, R. (1984) The Thrombins, p 166, CRC Press, Boca Raton, FL.
    • (1984) The Thrombins , pp. 166
    • Machovich, R.1
  • 2
    • 0000650903 scopus 로고
    • Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • Esmon, C. T., and Owen, W. G. (1981) Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C, Proc. Natl. Acad. Sci. U.S.A. 78, 2249-2252.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2249-2252
    • Esmon, C.T.1    Owen, W.G.2
  • 3
    • 0034615559 scopus 로고    scopus 로고
    • Regulation of blood coagulation
    • Esmon, C. T. (2000) Regulation of blood coagulation, Biochim. Biophys. Acta 1477, 349-360.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 349-360
    • Esmon, C.T.1
  • 4
    • 0023841049 scopus 로고
    • Evidence for multiple conformational changes in the active center of thrombin induced by complex formation with thrombomodulin: An analysis employing nitroxide spin-labels
    • Musci, G., Berliner, L. J., and Esmon, C. T. (1988) Evidence for multiple conformational changes in the active center of thrombin induced by complex formation with thrombomodulin: an analysis employing nitroxide spin-labels, Biochemistry 27, 769-773.
    • (1988) Biochemistry , vol.27 , pp. 769-773
    • Musci, G.1    Berliner, L.J.2    Esmon, C.T.3
  • 6
    • 0030848495 scopus 로고    scopus 로고
    • Site-specific dissection of substrate recognition by thrombin
    • Vindigni, A., Dang, Q. D., and Di Cera, E. (1997) Site-specific dissection of substrate recognition by thrombin, Nat. Biotechnol. 15, 891-895.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 891-895
    • Vindigni, A.1    Dang, Q.D.2    Di Cera, E.3
  • 7
    • 0034973468 scopus 로고    scopus 로고
    • Determinants of thrombin specificity
    • Di Cera, E., and Cantwell, A. M. (2001) Determinants of thrombin specificity, Ann. N.Y. Acad. Sci. 936, 133-146.
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 133-146
    • Di Cera, E.1    Cantwell, A.M.2
  • 9
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-Å resolution
    • Martin, P. D., Robertson, W., Turk, D., Huber, R., Bode, W., and Edwards, B. F. (1992) The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-Å resolution, J. Biol. Chem. 267, 7911-7920.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7911-7920
    • Martin, P.D.1    Robertson, W.2    Turk, D.3    Huber, R.4    Bode, W.5    Edwards, B.F.6
  • 10
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode, W., Turk, D., and Karshikov, A. (1992) The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships, Protein Sci. 1, 426-471.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 12
  • 13
    • 0033520366 scopus 로고    scopus 로고
    • Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains
    • Hall, S. W., Nagashima, M., Zhao, L., Morser, J., and Leung, L. L. K. (1999) Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains, J. Biol. Chem. 274, 25510-25516.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25510-25516
    • Hall, S.W.1    Nagashima, M.2    Zhao, L.3    Morser, J.4    Leung, L.L.K.5
  • 15
    • 0028023796 scopus 로고
    • Activation-induced exposure of the thrombin anion-binding exosite. Interactions of recombinant mutant prothrombins with thrombomodulin and a thrombin exosite-specific antibody
    • Wu, Q., Picard, V., Aiach, M., and Sadler, J. E. (1994) Activation-induced exposure of the thrombin anion-binding exosite. Interactions of recombinant mutant prothrombins with thrombomodulin and a thrombin exosite-specific antibody, J. Biol. Chem. 269, 3725-3730.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3725-3730
    • Wu, Q.1    Picard, V.2    Aiach, M.3    Sadler, J.E.4
  • 17
    • 0034636749 scopus 로고    scopus 로고
    • Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR-1 or protein C
    • Arosio, D., Ayala, Y. M., and Di Cera, E. (2000) Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR-1 or protein C, Biochemistry 39, 8095-8101.
    • (2000) Biochemistry , vol.39 , pp. 8095-8101
    • Arosio, D.1    Ayala, Y.M.2    Di Cera, E.3
  • 18
    • 0032553446 scopus 로고    scopus 로고
    • Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes
    • Myles, T., Church, F., Whinna, H., Monard, D., and Stone, S. R. (1998) Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes, J. Biol. Chem. 273, 31203-31208.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31203-31208
    • Myles, T.1    Church, F.2    Whinna, H.3    Monard, D.4    Stone, S.R.5
  • 19
    • 0028845757 scopus 로고
    • Protein C inhibitor is a potent inhibitor of the thrombin-thrombomodulin complex
    • Rezaie, A. R., Cooper, S. T., Church, F. C., and Esmon, C. T. (1995) Protein C inhibitor is a potent inhibitor of the thrombin-thrombomodulin complex, J. Biol. Chem. 270, 25336-25339.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25336-25339
    • Rezaie, A.R.1    Cooper, S.T.2    Church, F.C.3    Esmon, C.T.4
  • 20
    • 0032512433 scopus 로고    scopus 로고
    • Thrombomodulin increases the rate of thrombin inhibition by BPTI
    • Rezaie, A. R., He, X., and Esmon, C. T. (1998) Thrombomodulin increases the rate of thrombin inhibition by BPTI, Biochemistry 37, 693-699.
    • (1998) Biochemistry , vol.37 , pp. 693-699
    • Rezaie, A.R.1    He, X.2    Esmon, C.T.3
  • 21
    • 0027516679 scopus 로고
    • Evidence for common structural changes in thrombin induced by active-site or exosite binding
    • Parry, M. A., Stone, S. R., Hofsteenge, J., and Jackman, M. P. (1993) Evidence for common structural changes in thrombin induced by active-site or exosite binding, Biochem. J. 290, 665-670.
    • (1993) Biochem. J. , vol.290 , pp. 665-670
    • Parry, M.A.1    Stone, S.R.2    Hofsteenge, J.3    Jackman, M.P.4
  • 22
    • 0026351350 scopus 로고
    • The active site of thrombin is altered upon binding to thrombomodulin
    • Ye, J., Esmon, N. L., Esmon, C. T., and Johnson, A. E. (1991) The active site of thrombin is altered upon binding to thrombomodulin, J. Biol. Chem. 266, 23016-23021.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23016-23021
    • Ye, J.1    Esmon, N.L.2    Esmon, C.T.3    Johnson, A.E.4
  • 24
    • 0025338124 scopus 로고
    • Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects
    • Ni, F., Konishi, Y., and Scheraga, H. A. (1990) Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects, Biochemistry 29, 4479-4489.
    • (1990) Biochemistry , vol.29 , pp. 4479-4489
    • Ni, F.1    Konishi, Y.2    Scheraga, H.A.3
  • 25
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • Mandell, J. G., Falick, A. M., and Komives, E. A. (1998) Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry, Anal. Chem. 70, 3987-3995.
    • (1998) Anal. Chem. , vol.70 , pp. 3987-3995
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 26
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein-protein interfaces by decreased amide proton solvent accessibility
    • Mandell, J. G., Falick, A. M., and Komives, E. A. (1998) Identification of protein-protein interfaces by decreased amide proton solvent accessibility, Proc. Natl. Acad. Sci. U.S.A. 95, 14705-14710.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14705-14710
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 27
    • 0035815111 scopus 로고    scopus 로고
    • Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB
    • Hughes, C. A., Mandell, J. G., Anand, G. S., Stock, A. M., and Komives, E. A. (2001) Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB, J. Mol. Biol. 307, 967-976.
    • (2001) J. Mol. Biol. , vol.307 , pp. 967-976
    • Hughes, C.A.1    Mandell, J.G.2    Anand, G.S.3    Stock, A.M.4    Komives, E.A.5
  • 28
    • 0034681302 scopus 로고    scopus 로고
    • Electrostatic dependence of the thrombin-thrombomodulin interaction
    • Baerga-Ortiz, A., Rezaie, A. R., and Komives, E. A. (2000) Electrostatic dependence of the thrombin-thrombomodulin interaction, J. Mol. Biol. 296, 651-658.
    • (2000) J. Mol. Biol. , vol.296 , pp. 651-658
    • Baerga-Ortiz, A.1    Rezaie, A.R.2    Komives, E.A.3
  • 29
    • 0035969987 scopus 로고    scopus 로고
    • Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange
    • Hoofnagle, A. N., Resing, K. A., Goldsmith, E. J., and Ahn, N. G. (2001) Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange, Proc. Natl. Acad. Sci. U.S.A. 98, 956-961.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 956-961
    • Hoofnagle, A.N.1    Resing, K.A.2    Goldsmith, E.J.3    Ahn, N.G.4
  • 30
    • 0036025308 scopus 로고    scopus 로고
    • 2H exchange reveals communication between the cAMP and the catalytic subunit binding sites in the regulatory subunit of protein kinase A
    • 2H exchange reveals communication between the cAMP and the catalytic subunit binding sites in the regulatory subunit of protein kinase A, J. Mol. Biol. 323, 377-386.
    • (2002) J. Mol. Biol. , vol.323 , pp. 377-386
    • Anand, G.S.1    Hughes, C.A.2    Jones, J.M.3    Taylor, S.S.4    Komives, E.A.5
  • 31
    • 0024294306 scopus 로고
    • Enzymatic properties of proteolytic derivatives of human alpha-thrombin
    • Hofsteenge, J., Braun, P. J., and Stone, S. R. (1988) Enzymatic properties of proteolytic derivatives of human alpha-thrombin, Biochemistry 27, 2144-2151.
    • (1988) Biochemistry , vol.27 , pp. 2144-2151
    • Hofsteenge, J.1    Braun, P.J.2    Stone, S.R.3
  • 32
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel, G. M., Lockless, S. W., Wall, M. A., and Ranganathan, R. (2002) Evolutionarily conserved networks of residues mediate allosteric communication in proteins, Nat. Struct. Biol. 10, 59-68.
    • (2002) Nat. Struct. Biol. , vol.10 , pp. 59-68
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.