메뉴 건너뛰기




Volumn 48, Issue 34, 2009, Pages 8261-8270

Mutagenesis studies toward understanding allostery in thrombin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; ACTIVE SITE; ALLOSTERY; AMIDOLYTIC ACTIVITIES; BINDING LOOP; CATALYTIC ACTIVITY; CATALYTIC RESIDUE; COFACTOR BINDING; COFACTORS; CYS RESIDUES; DISULFIDE BONDS; MAMMALIAN CELLS; SUBSTRATE SPECIFICITY; THROMBOMODULIN;

EID: 69249094653     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900921t     Document Type: Article
Times cited : (13)

References (64)
  • 1
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • Mann, K. G., Jenny, R. J., and Krishnaswamy, S. (1988) Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annu. Rev. Biochem. 57, 915-956.
    • (1988) Annu. Rev. Biochem , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 2
    • 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
  • 3
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance and regulation
    • Davie, E. W., Fujikawa, K, and Kisiel, W. (1991) The coagulation cascade: Initiation, maintenance and regulation. Biochemistry 30, 10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 4
    • 0029014036 scopus 로고
    • An allosteric switch controls the procoagulant and anticoagulant activities of thrombin
    • Dang, Q. D., Vindigni, A., and Di Cera, E. (1995) An allosteric switch controls the procoagulant and anticoagulant activities of thrombin. Proc. Natl. Acad. Sci. U.S.A. 92, 5977-5981.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 5977-5981
    • Dang, Q.D.1    Vindigni, A.2    Di Cera, E.3
  • 6
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon, C. T. (1993) Molecular events that control the protein C anticoagulant pathway. Thromb. Haemost. 70, 1-5.
    • (1993) Thromb. Haemost , vol.70 , pp. 1-5
    • Esmon, C.T.1
  • 7
    • 0026775230 scopus 로고
    • Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity
    • Tsiang, M., Lentz, S., and Sadler, J. E. (1992) Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity. J. Biol. Chem. 267, 6164-6170.
    • (1992) J. Biol. Chem , vol.267 , pp. 6164-6170
    • Tsiang, M.1    Lentz, S.2    Sadler, J.E.3
  • 8
    • 20444427991 scopus 로고    scopus 로고
    • The anticoagulant protein C pathway
    • Dahlbäck, B., and Villoutreix, B. O. (2005) The anticoagulant protein C pathway. FEBS Lett. 579, 3310-3316.
    • (2005) FEBS Lett , vol.579 , pp. 3310-3316
    • Dahlbäck, B.1    Villoutreix, B.O.2
  • 9
    • 27744530963 scopus 로고    scopus 로고
    • Thrombomodulin tightens the thrombin active site loop to promote protein C activation
    • Koeppe, J. R., Seitova, A., Mather, T., and Komives, E. A. (2005) Thrombomodulin tightens the thrombin active site loop to promote protein C activation. Biochemistry 44, 14784-14791.
    • (2005) Biochemistry , vol.44 , pp. 14784-14791
    • Koeppe, J.R.1    Seitova, A.2    Mather, T.3    Komives, E.A.4
  • 10
    • 0026704809 scopus 로고
    • Regulation of blood coagulation by the protein C system
    • Walker, F. J., and Fay, P. J. (1992) Regulation of blood coagulation by the protein C system. FASEB J. 6, 2561-2567.
    • (1992) FASEB J , vol.6 , pp. 2561-2567
    • Walker, F.J.1    Fay, P.J.2
  • 11
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. W. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4803.
    • (2002) Chem. Rev , vol.102 , pp. 4751-4803
    • Gettins, P.G.W.1
  • 12
    • 41149167073 scopus 로고    scopus 로고
    • Structural identification of the pathway of long-range communication in an allosteric enzyme
    • Gandhi, P. S., Chen, Z., Mathews, F. S., and Di Cera, E. (2008) Structural identification of the pathway of long-range communication in an allosteric enzyme. Proc. Natl. Acad. Sci. U.S.A. 105, 1832-1837.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 1832-1837
    • Gandhi, P.S.1    Chen, Z.2    Mathews, F.S.3    Di Cera, E.4
  • 13
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs, M. T., and Bode, W. (1993) A player of many parts: The spotlight falls on thrombin's structure. Thromb. Res. 69, 1-58.
    • (1993) Thromb. Res , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 14
    • 0024542430 scopus 로고
    • Microthrombomodulin: Residues 310-486 from the epidermal growth factor precursor homology domain of thrombomodulin will accelerate protein C activation
    • Stearns, D. J., Kurosawa, S., and Esmon, C. T. (1989) Microthrombomodulin: Residues 310-486 from the epidermal growth factor precursor homology domain of thrombomodulin will accelerate protein C activation. J. Biol. Chem. 264, 3352-3356.
    • (1989) J. Biol. Chem , vol.264 , pp. 3352-3356
    • Stearns, D.J.1    Kurosawa, S.2    Esmon, C.T.3
  • 16
    • 0033135017 scopus 로고    scopus 로고
    • Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site-directed mutagenesis, and computer modeling
    • Knobe, K., Berntsdotter, A., Shen, L., Morser, J., Dahlbäck, B., and Villoutreix, B. O. (1999) Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site-directed mutagenesis, and computer modeling. Proteins 35, 218-234.
    • (1999) Proteins , vol.35 , pp. 218-234
    • Knobe, K.1    Berntsdotter, A.2    Shen, L.3    Morser, J.4    Dahlbäck, B.5    Villoutreix, B.O.6
  • 17
    • 0024396997 scopus 로고
    • The last three consecutive epidermal growth factor-like structures of human thrombomodulin comprise the minimum functional domain for protein C-activating cofactor activity and anticoagulant activity
    • Zushi, M., Gomi, K., Yamamoto, S., Maruyama, I., Hayashi, T., and Suzuki, K. (1989) The last three consecutive epidermal growth factor-like structures of human thrombomodulin comprise the minimum functional domain for protein C-activating cofactor activity and anticoagulant activity. J. Biol. Chem. 264, 10351-10353.
    • (1989) J. Biol. Chem , vol.264 , pp. 10351-10353
    • Zushi, M.1    Gomi, K.2    Yamamoto, S.3    Maruyama, I.4    Hayashi, T.5    Suzuki, K.6
  • 18
    • 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
  • 19
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 21
    • 0034701009 scopus 로고    scopus 로고
    • Sodium binding site of factor Xa: Role of sodium in the prothrombinase complex
    • Rezaie, A. R., and He, X. (2000) Sodium binding site of factor Xa: Role of sodium in the prothrombinase complex. Biochemistry 39, 1817-1825.
    • (2000) Biochemistry , vol.39 , pp. 1817-1825
    • Rezaie, A.R.1    He, X.2
  • 22
    • 0033582504 scopus 로고    scopus 로고
    • He, X., and Rezaie, A. R. (1999) Identification and characterization of the sodium-binding site of activated protein C. J. Biol. Chem. 274, 4970-4976.
    • He, X., and Rezaie, A. R. (1999) Identification and characterization of the sodium-binding site of activated protein C. J. Biol. Chem. 274, 4970-4976.
  • 24
    • 0037020083 scopus 로고    scopus 로고
    • Prothrombinase assembly and S1 site occupancy restore the catalytic activity of FXa impaired by mutation at the sodium-binding site
    • Camire, R. M. (2002) Prothrombinase assembly and S1 site occupancy restore the catalytic activity of FXa impaired by mutation at the sodium-binding site. J. Biol. Chem. 277, 37863-37870.
    • (2002) J. Biol. Chem , vol.277 , pp. 37863-37870
    • Camire, R.M.1
  • 26
  • 27
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine beta-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0
    • Bode, W., and Schwager, P. (1975) The refined crystal structure of bovine beta-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J. Mol. Biol. 98, 693-717.
    • (1975) J. Mol. Biol , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 29
    • 0028168831 scopus 로고
    • 2+ binding site yet retains function
    • 2+ binding site yet retains function. J. Biol. Chem. 269, 21495-21499.
    • (1994) J. Biol. Chem , vol.269 , pp. 21495-21499
    • Rezaie, A.R.1    Esmon, C.T.2
  • 30
    • 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
  • 31
    • 0142091399 scopus 로고    scopus 로고
    • Thrombomodulin allosterically modulates the activity of the anticoagulant thrombin
    • Rezaie, A. R., and Yang, L. (2003) Thrombomodulin allosterically modulates the activity of the anticoagulant thrombin. Proc. Natl. Acad. Sci. U.S.A. 100, 12051-12056.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 12051-12056
    • Rezaie, A.R.1    Yang, L.2
  • 33
    • 2942703945 scopus 로고    scopus 로고
    • Crystal Structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery
    • Carter, W. J., Myles, T., Gibbs, C. S., Leung, L. L., and Huntington, J. A. (2004) Crystal Structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery. Biol. Chem. 279, 26387-26394.
    • (2004) Biol. Chem , vol.279 , pp. 26387-26394
    • Carter, W.J.1    Myles, T.2    Gibbs, C.S.3    Leung, L.L.4    Huntington, J.A.5
  • 34
    • 0026351350 scopus 로고
    • The active site of thrombin is altered upon binding to thrombomodulin: Two distinct structural changes are detected by fluorescence, but only one correlates with protein C activation
    • Ye, J., Esmon, N. L., Esmon, C. T., and Johnson, A. E. (1991) The active site of thrombin is altered upon binding to thrombomodulin: Two distinct structural changes are detected by fluorescence, but only one correlates with protein C activation. 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
  • 35
    • 32244444849 scopus 로고    scopus 로고
    • Activation of protein C by the thrombin-thrombomodulin complex: Cooperative roles of Arg-35 of thrombin and Arg-67 of protein C
    • Yang, L., Manithody, C., and Rezaie, A. R. (2006) Activation of protein C by the thrombin-thrombomodulin complex: Cooperative roles of Arg-35 of thrombin and Arg-67 of protein C. Proc. Natl. Acad. Sci. U.S.A. 103, 879-884.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 879-884
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 36
    • 0030029895 scopus 로고    scopus 로고
    • Tryptophan60-D in the B-insertion loop of thrombin modulates the thrombin-antithrombin reaction
    • Rezaie, A. R. (1996) Tryptophan60-D in the B-insertion loop of thrombin modulates the thrombin-antithrombin reaction. Biochemistry 35, 1918-1924.
    • (1996) Biochemistry , vol.35 , pp. 1918-1924
    • Rezaie, A.R.1
  • 37
    • 0031913779 scopus 로고    scopus 로고
    • Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin-induced conformers of antithrombin
    • Rezaie, A. R. (1998) Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin-induced conformers of antithrombin. Protein Sci. 7, 349-357.
    • (1998) Protein Sci , vol.7 , pp. 349-357
    • Rezaie, A.R.1
  • 38
    • 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. 290, 651-658.
    • (2000) J. Mol. Biol , vol.290 , pp. 651-658
    • Baerga-Ortiz, A.1    Rezaie, A.R.2    Komives, E.A.3
  • 39
    • 0027078511 scopus 로고
    • The function of calcium in protein C activation by thrombin and the thrombin-thrombomodulin complex can be distinguished by mutational analysis of protein C derivatives
    • Rezaie, A. R., and Esmon, C. T. (1992) The function of calcium in protein C activation by thrombin and the thrombin-thrombomodulin complex can be distinguished by mutational analysis of protein C derivatives. J. Biol. Chem. 267, 26104-26109.
    • (1992) J. Biol. Chem , vol.267 , pp. 26104-26109
    • Rezaie, A.R.1    Esmon, C.T.2
  • 40
    • 0034595843 scopus 로고    scopus 로고
    • Role of proexosite I in factor Va-dependent substrate interactions of prothrombin activation
    • Anderson, P. J., Nesset, A., Dharmawardana, K. R., and Bock, P. E. (2000) Role of proexosite I in factor Va-dependent substrate interactions of prothrombin activation. J. Biol. Chem. 275, 16435-16442.
    • (2000) J. Biol. Chem , vol.275 , pp. 16435-16442
    • Anderson, P.J.1    Nesset, A.2    Dharmawardana, K.R.3    Bock, P.E.4
  • 43
    • 0037184970 scopus 로고    scopus 로고
    • Localization of the heparin binding exosite of factor IXa
    • Yang, L., Manithody, C., and Rezaie, A. R. (2002) Localization of the heparin binding exosite of factor IXa. J. Biol. Chem. 277, 50756-50760.
    • (2002) J. Biol. Chem , vol.277 , pp. 50756-50760
    • Yang, L.1    Manithody, C.2    Rezaie, A.R.3
  • 45
    • 0031053642 scopus 로고    scopus 로고
    • Contribution of Lysine 60f to S1′ specificity of thrombin
    • Rezaie, A. R., and Olson, S. T. (1997) Contribution of Lysine 60f to S1′ specificity of thrombin. Biochemistry 36, 1026-1033.
    • (1997) Biochemistry , vol.36 , pp. 1026-1033
    • Rezaie, A.R.1    Olson, S.T.2
  • 49
    • 33846823909 scopus 로고
    • An N.log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) 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
  • 51
    • 0041784950 scopus 로고    scopus 로고
    • MacKerel, A. D. Jr., Bashford, D., Bellot, M., Dunbrack, R. L. Jr., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph-McCarthy, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, W. E.III, Roux, B., Schlenkrich, M., Smith, J. C., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. 102, 3286-3616.
    • MacKerel, A. D. Jr., Bashford, D., Bellot, M., Dunbrack, R. L. Jr., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph-McCarthy, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, W. E.III, Roux, B., Schlenkrich, M., Smith, J. C., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. 102, 3286-3616.
  • 53
    • 0037518132 scopus 로고    scopus 로고
    • Yang, L., and Rezaie, A. R. (2003) The fourth epidermal growth factor-like domain of thrombomodulin interacts with the basic exosite of protein C. J. Biol. Chem. 278, 484-10490.
    • Yang, L., and Rezaie, A. R. (2003) The fourth epidermal growth factor-like domain of thrombomodulin interacts with the basic exosite of protein C. J. Biol. Chem. 278, 484-10490.
  • 54
    • 0037200049 scopus 로고    scopus 로고
    • The thrombin epitope recognizing thrombomodulin is highly cooperative hot spot in exosite I
    • Pineda, A. O., Cantwell, A. M., Bush, L. A., Rose, T., and Di Cera, E. (2002) The thrombin epitope recognizing thrombomodulin is highly cooperative hot spot in exosite I. J. Biol. Chem. 277, 32015-32019.
    • (2002) J. Biol. Chem , vol.277 , pp. 32015-32019
    • Pineda, A.O.1    Cantwell, A.M.2    Bush, L.A.3    Rose, T.4    Di Cera, E.5
  • 55
    • 0025730441 scopus 로고
    • Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models
    • Olson, S. T., Halvorson, H. R., and Bjork, I. (1991) Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models. J. Biol. Chem. 266, 6342-6352.
    • (1991) J. Biol. Chem , vol.266 , pp. 6342-6352
    • Olson, S.T.1    Halvorson, H.R.2    Bjork, I.3
  • 56
    • 0242666308 scopus 로고    scopus 로고
    • Effects of activation peptide bond cleavage and fragment 2 interaction on the pathway of exosite 1 expression during activation of human prethrombin 1 to thrombin
    • Anderson, P. J., Nesset, A., and Bock, P. E. (2003) Effects of activation peptide bond cleavage and fragment 2 interaction on the pathway of exosite 1 expression during activation of human prethrombin 1 to thrombin. J. Biol. Chem. 278, 44482-44488.
    • (2003) J. Biol. Chem , vol.278 , pp. 44482-44488
    • Anderson, P.J.1    Nesset, A.2    Bock, P.E.3
  • 59
    • 34848874846 scopus 로고    scopus 로고
    • Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery
    • Bush-Pelc, L. A., Marino, F., Chen, Z., Pineda, A. O., Mathews, F. S., and Di Cera, E. (2007) Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery. J. Biol. Chem. 282, 27165-27170.
    • (2007) J. Biol. Chem , vol.282 , pp. 27165-27170
    • Bush-Pelc, L.A.1    Marino, F.2    Chen, Z.3    Pineda, A.O.4    Mathews, F.S.5    Di Cera, E.6
  • 60
    • 0026799442 scopus 로고
    • The active site of factor IXa is located far above the membrane surface and its conformation is altered upon association with factor VIIIa: A fluorescence study
    • Mutucumarana, V. P., Duffy, E. J., Lollar, P., and Johnson, A. E. (1992) The active site of factor IXa is located far above the membrane surface and its conformation is altered upon association with factor VIIIa: A fluorescence study. J. Biol. Chem. 267, 17012-17021.
    • (1992) J. Biol. Chem , vol.267 , pp. 17012-17021
    • Mutucumarana, V.P.1    Duffy, E.J.2    Lollar, P.3    Johnson, A.E.4
  • 61
    • 34547466613 scopus 로고    scopus 로고
    • crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4
    • Bah, A., Chen, Z., Bush-Pelc, L. A., Mathews, F. S., and Di Cera, E. (2007) crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4. Proc. Natl. Acad. Sci. U.S.A. 104, 11603-11608.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 11603-11608
    • Bah, A.1    Chen, Z.2    Bush-Pelc, L.A.3    Mathews, F.S.4    Di Cera, E.5
  • 62
    • 0030830185 scopus 로고    scopus 로고
    • Evidence for allosteric linkage between exosites 1 and 2 of thrombin
    • Fredenburgh, J. C., Stafford, A. R., and Weitz, J. (1997) Evidence for allosteric linkage between exosites 1 and 2 of thrombin. J. Biol. Chem. 272, 25493-25499.
    • (1997) J. Biol. Chem , vol.272 , pp. 25493-25499
    • Fredenburgh, J.C.1    Stafford, A.R.2    Weitz, J.3
  • 63
    • 0036510533 scopus 로고    scopus 로고
    • Binding of exosite ligands to human thrombin. Re-evaluation of allosteric linkage between thrombin exosite I and II
    • Verhamme, I. M., Olson, S. T., Tollefsen, D. M., and Bock, P. E. (2002) Binding of exosite ligands to human thrombin. Re-evaluation of allosteric linkage between thrombin exosite I and II. J. Biol. Chem. 277, 6788-6798.
    • (2002) J. Biol. Chem , vol.277 , pp. 6788-6798
    • Verhamme, I.M.1    Olson, S.T.2    Tollefsen, D.M.3    Bock, P.E.4
  • 64
    • 0027288125 scopus 로고
    • Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin
    • Arni, R. K., Padmanabhan, K., Padmanabhan, K. P., Wu, T.-P., and Tulinsky, A. (1993) Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin. Biochemistry 32, 4727-4737.
    • (1993) Biochemistry , vol.32 , pp. 4727-4737
    • Arni, R.K.1    Padmanabhan, K.2    Padmanabhan, K.P.3    Wu, T.-P.4    Tulinsky, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.