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Volumn 36, Issue 2, 2006, Pages 122-130

Structure and interaction modes of thrombin

Author keywords

Anion binding exosite; Coagulation; Cofactors; Crystal structures; Fibrin; Specificity; Thrombin; Thrombomodulin

Indexed keywords

CARBOHYDRATE; RECEPTOR PROTEIN; THROMBIN;

EID: 33645353328     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2005.12.027     Document Type: Article
Times cited : (92)

References (98)
  • 1
    • 0346435111 scopus 로고    scopus 로고
    • A brief historical review of the waterfall/cascade of blood coagulation
    • E.W. Davie A brief historical review of the waterfall/cascade of blood coagulation J. Biol. Chem. 278 2003 50819
    • (2003) J. Biol. Chem. , vol.278 , pp. 50819
    • Davie, E.W.1
  • 2
    • 0026476381 scopus 로고
    • Thrombin is a Na(+)-activated enzyme
    • C.M. Wells, and E. Di Cera Thrombin is a Na(+)-activated enzyme Biochemistry 31 1992 11721
    • (1992) Biochemistry , vol.31 , pp. 11721
    • Wells, C.M.1    Di Cera, E.2
  • 3
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • S.R. Coughlin Protease-activated receptors in hemostasis, thrombosis and vascular biology J. Thromb. Haemost. 3 2005 1800 1814
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1800-1814
    • Coughlin, S.R.1
  • 4
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • C.T. Esmon The roles of protein C and thrombomodulin in the regulation of blood coagulation J. Biol. Chem. 264 1989 4743
    • (1989) J. Biol. Chem. , vol.264 , pp. 4743
    • Esmon, C.T.1
  • 5
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • L. Bajzar, J. Morser, and M. Nesheim TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex J. Biol. Chem. 271 1996 16603
    • (1996) J. Biol. Chem. , vol.271 , pp. 16603
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 6
    • 0024431034 scopus 로고
    • The refined 1.9 a crystal structure of human alpha-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • W. Bode, I. Mayr, and U. Baumann The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment EMBO J. 8 1989 3467
    • (1989) EMBO J. , vol.8 , pp. 3467
    • Bode, W.1    Mayr, I.2    Baumann, U.3
  • 7
    • 0027050807 scopus 로고
    • The refined 1.9-A 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
    • W. Bode, D. Turk, and A. Karshikov The refined 1.9-A 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 1992 426
    • (1992) Protein Sci. , vol.1 , pp. 426
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 8
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • M.T. Stubbs, and W. Bode A player of many parts: the spotlight falls on thrombin's structure Thromb. Res. 69 1993 1
    • (1993) Thromb. Res. , vol.69 , pp. 1
    • Stubbs, M.T.1    Bode, W.2
  • 9
    • 0028912561 scopus 로고
    • The clot thickens: Clues provided by thrombin structure
    • M.T. Stubbs, and W. Bode The clot thickens: clues provided by thrombin structure Trends Biochem. Sci. 20 1995 23
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 23
    • Stubbs, M.T.1    Bode, W.2
  • 10
    • 0030811924 scopus 로고    scopus 로고
    • Comparative analysis of haemostatic proteinases: Structural aspects of thrombin, factor Xa, factor IXa and protein C
    • W. Bode, H. Brandstetter, T. Mather, and M.T. Stubbs Comparative analysis of haemostatic proteinases: structural aspects of thrombin, factor Xa, factor IXa and protein C Thromb. Haemost. 78 1997 501
    • (1997) Thromb. Haemost. , vol.78 , pp. 501
    • Bode, W.1    Brandstetter, H.2    Mather, T.3    Stubbs, M.T.4
  • 11
    • 27144505651 scopus 로고    scopus 로고
    • Molecular recognition mechanisms of thrombin
    • J.A. Huntington Molecular recognition mechanisms of thrombin J. Thromb. Haemost. 3 2005 1861
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1861
    • Huntington, J.A.1
  • 12
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding: II. the binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen
    • W. Bode The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding: II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen J. Mol. Biol. 127 1979 357
    • (1979) J. Mol. Biol. , vol.127 , pp. 357
    • Bode, W.1
  • 13
    • 0028586082 scopus 로고
    • The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin
    • J. Vijayalakshmi, K.P. Padmanabhan, K.G. Mann, and A. Tulinsky The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: changes accompanying activation and exosite binding to thrombin Protein Sci. 3 1994 2254
    • (1994) Protein Sci. , vol.3 , pp. 2254
    • Vijayalakshmi, J.1    Padmanabhan, K.P.2    Mann, K.G.3    Tulinsky, A.4
  • 15
    • 0028884430 scopus 로고
    • Identification of residues linked to the slow→fast transition of thrombin
    • E.R. Guinto, A. Vindigni, and Y.M. Ayala Identification of residues linked to the slow→fast transition of thrombin Proc. Natl. Acad. Sci. U. S. A. 92 1995 11185
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11185
    • Guinto, E.R.1    Vindigni, A.2    Ayala, Y.M.3
  • 16
    • 0025837452 scopus 로고
    • Crystallographic analysis at 3.0-A resolution of the binding to human thrombin of four active site-directed inhibitors
    • D.W. Banner, and P. Hadvary Crystallographic analysis at 3.0-A resolution of the binding to human thrombin of four active site-directed inhibitors J. Biol. Chem. 266 1991 20085
    • (1991) J. Biol. Chem. , vol.266 , pp. 20085
    • Banner, D.W.1    Hadvary, P.2
  • 17
    • 0026465007 scopus 로고
    • Refined 2.3 a X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. a starting point for improving antithrombotics
    • H. Brandstetter, D. Turk, and H.W. Hoeffken Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics J. Mol. Biol. 226 1992 1085
    • (1992) J. Mol. Biol. , vol.226 , pp. 1085
    • Brandstetter, H.1    Turk, D.2    Hoeffken, H.W.3
  • 18
    • 0026548768 scopus 로고
    • The interaction of thrombin with fibrinogen. a structural basis for its specificity
    • M.T. Stubbs, H. Oschkinat, and I. Mayr The interaction of thrombin with fibrinogen. A structural basis for its specificity Eur. J. Biochem. 206 1992 187
    • (1992) Eur. J. Biochem. , vol.206 , pp. 187
    • Stubbs, M.T.1    Oschkinat, H.2    Mayr, I.3
  • 19
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the a alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution
    • P.D. Martin, W. Robertson, and D. Turk The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution J. Biol. Chem. 267 1992 7911
    • (1992) J. Biol. Chem. , vol.267 , pp. 7911
    • Martin, P.D.1    Robertson, W.2    Turk, D.3
  • 20
    • 0034711216 scopus 로고    scopus 로고
    • Interaction of the factor XIII activation peptide with alpha-thrombin. Crystal structure of its enzyme-substrate analog complex
    • C. Sadasivan, and V.C. Yee Interaction of the factor XIII activation peptide with alpha-thrombin. Crystal structure of its enzyme-substrate analog complex J. Biol. Chem. 275 2000 36942
    • (2000) J. Biol. Chem. , vol.275 , pp. 36942
    • Sadasivan, C.1    Yee, V.C.2
  • 21
    • 0021080275 scopus 로고
    • Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen
    • T.J. Janus, S.D. Lewis, L. Lorand, and J.A. Shafer Promotion of thrombin-catalyzed activation of factor XIII by fibrinogen Biochemistry 22 1983 6269
    • (1983) Biochemistry , vol.22 , pp. 6269
    • Janus, T.J.1    Lewis, S.D.2    Lorand, L.3    Shafer, J.A.4
  • 22
    • 0025923430 scopus 로고
    • Glu-192-Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin
    • B.F. Le Bonniec, and C.T. Esmon Glu-192-Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin Proc. Natl. Acad. Sci. U. S. A. 88 1991 7371
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7371
    • Le Bonniec, B.F.1    Esmon, C.T.2
  • 23
    • 0030959346 scopus 로고    scopus 로고
    • The thrombin E192Q-BPTI complex reveals gross structural rearrangements: Implications for the interaction with antithrombin and thrombomodulin
    • A. Van de Locht, W. Bode, and R. Huber The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin EMBO J. 16 1997 2977
    • (1997) EMBO J. , vol.16 , pp. 2977
    • Van De Locht, A.1    Bode, W.2    Huber, R.3
  • 24
    • 0028084791 scopus 로고
    • Molecular recognition by thrombin. Role of the slow→fast transition, site-specific ion binding energetics and thermodynamic mapping of structural components
    • Y. Ayala, and E. Di Cera Molecular recognition by thrombin. Role of the slow→fast transition, site-specific ion binding energetics and thermodynamic mapping of structural components J. Mol. Biol. 235 1994 733
    • (1994) J. Mol. Biol. , vol.235 , pp. 733
    • Ayala, Y.1    Di Cera, E.2
  • 27
    • 3843133006 scopus 로고    scopus 로고
    • Molecular dissection of Na+ binding to thrombin
    • A.O. Pineda, C.J. Carrell, and L.A. Bush Molecular dissection of Na+ binding to thrombin J. Biol. Chem. 279 2004 31842
    • (2004) J. Biol. Chem. , vol.279 , pp. 31842
    • Pineda, A.O.1    Carrell, C.J.2    Bush, L.A.3
  • 28
    • 0037387204 scopus 로고    scopus 로고
    • The molecular basis of thrombin allostery revealed by a 1.8 a structure of the "slow" form
    • J.A. Huntington, and C.T. Esmon The molecular basis of thrombin allostery revealed by a 1.8 A structure of the "slow" form Structure (Camb). 11 2003 469
    • (2003) Structure (Camb). , vol.11 , pp. 469
    • Huntington, J.A.1    Esmon, C.T.2
  • 29
    • 2942703945 scopus 로고    scopus 로고
    • Crystal structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery
    • W.J. Carter, T. Myles, and C.S. Gibbs Crystal structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery J. Biol. Chem. 279 2004 26387
    • (2004) J. Biol. Chem. , vol.279 , pp. 26387
    • Carter, W.J.1    Myles, T.2    Gibbs, C.S.3
  • 30
    • 25144446242 scopus 로고    scopus 로고
    • Effect of Na+ binding on the conformation, stability and molecular recognition properties of thrombin
    • V. De Filippis, E. De Dea, F. Lucatello, and R. Frasson Effect of Na+ binding on the conformation, stability and molecular recognition properties of thrombin Biochem. J. 390 2005 485
    • (2005) Biochem. J. , vol.390 , pp. 485
    • De Filippis, V.1    De Dea, E.2    Lucatello, F.3    Frasson, R.4
  • 31
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine beta-trypsin at 1.8 a resolution: II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0
    • W. Bode, and P. Schwager The refined crystal structure of bovine beta-trypsin at 1.8 A resolution: II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0 J. Mol. Biol. 98 1975 693 717
    • (1975) J. Mol. Biol. , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 32
    • 0025329390 scopus 로고
    • The structure of a complex of recombinant hirudin and human alpha-thrombin
    • T.J. Rydel, K.G. Ravichandran, and A. Tulinsky The structure of a complex of recombinant hirudin and human alpha-thrombin Science 249 1990 277
    • (1990) Science , vol.249 , pp. 277
    • Rydel, T.J.1    Ravichandran, K.G.2    Tulinsky, A.3
  • 33
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • T.J. Rydel, A. Tulinsky, W. Bode, and R. Huber Refined structure of the hirudin-thrombin complex J. Mol. Biol. 221 1991 583
    • (1991) J. Mol. Biol. , vol.221 , pp. 583
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 34
    • 0025309452 scopus 로고
    • Crystal structure of the thrombin-hirudin complex: A novel mode of serine protease inhibition
    • M.G. Grütter, J.P. Priestle, and J. Rahuel Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition EMBO J. 9 1990 2361
    • (1990) EMBO J. , vol.9 , pp. 2361
    • Grütter, M.G.1    Priestle, J.P.2    Rahuel, J.3
  • 36
    • 22844449689 scopus 로고    scopus 로고
    • Hirudin binding reveals key determinants of thrombin allostery
    • K.E. Mengwasser, L.A. Bush, and P. Shih Hirudin binding reveals key determinants of thrombin allostery J. Biol. Chem. 280 2005 26997
    • (2005) J. Biol. Chem. , vol.280 , pp. 26997
    • Mengwasser, K.E.1    Bush, L.A.2    Shih, P.3
  • 37
    • 0028784163 scopus 로고
    • Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • A. van de Locht, D. Lamba, and M. Bauer Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin EMBO J. 14 1995 5149
    • (1995) EMBO J. , vol.14 , pp. 5149
    • Van De Locht, A.1    Lamba, D.2    Bauer, M.3
  • 38
    • 0029957955 scopus 로고    scopus 로고
    • The ornithodorin-thrombin crystal structure, a key to the TAP enigma?
    • A. van de Locht, M.T. Stubbs, and W. Bode The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J. 15 1996 6011
    • (1996) EMBO J. , vol.15 , pp. 6011
    • Van De Locht, A.1    Stubbs, M.T.2    Bode, W.3
  • 39
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug
    • P. Fuentes-Prior, C. Noeske-Jungblut, and P. Donner Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug Proc. Natl. Acad. Sci. U. S. A. 94 1997 11845
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11845
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3
  • 40
    • 1542297770 scopus 로고    scopus 로고
    • Crystal structure of the complex between thrombin and the central "e" region of fibrin
    • I. Pechik, J. Madrazo, and M.W. Mosesson Crystal structure of the complex between thrombin and the central "E" region of fibrin Proc. Natl. Acad. Sci. U. S. A. 101 2004 2718
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2718
    • Pechik, I.1    Madrazo, J.2    Mosesson, M.W.3
  • 41
    • 0037205399 scopus 로고    scopus 로고
    • Substrate recognition drives the evolution of serine proteases
    • T. Rose, and E. Di Cera Substrate recognition drives the evolution of serine proteases J. Biol. Chem. 277 2002 19243
    • (2002) J. Biol. Chem. , vol.277 , pp. 19243
    • Rose, T.1    Di Cera, E.2
  • 42
    • 0029819059 scopus 로고    scopus 로고
    • Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen a alpha: Geometry of the catalytic triad and interactions of the P1′, P2′, and P3′ substrate residues
    • P.D. Martin, M.G. Malkowski, and J. DiMaio Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen A alpha: geometry of the catalytic triad and interactions of the P1′, P2′, and P3′ substrate residues Biochemistry 35 1996 13030
    • (1996) Biochemistry , vol.35 , pp. 13030
    • Martin, P.D.1    Malkowski, M.G.2    Dimaio, J.3
  • 43
    • 0026072517 scopus 로고
    • Domains specifying thrombin-receptor interaction
    • T.K. Vu, V.I. Wheaton, and D.T. Hung Domains specifying thrombin-receptor interaction Nature 353 1991 674
    • (1991) Nature , vol.353 , pp. 674
    • Vu, T.K.1    Wheaton, V.I.2    Hung, D.T.3
  • 44
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • S.R. Coughlin Protease-activated receptors in hemostasis, thrombosis and vascular biology J. Thromb. Haemost. 3 2005 1800
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1800
    • Coughlin, S.R.1
  • 45
    • 0028209977 scopus 로고
    • Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes
    • I.I. Mathews, K.P. Padmanabhan, and V. Ganesh Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes Biochemistry 33 1994 3266
    • (1994) Biochemistry , vol.33 , pp. 3266
    • Mathews, I.I.1    Padmanabhan, K.P.2    Ganesh, V.3
  • 46
    • 0035501805 scopus 로고    scopus 로고
    • Molecular mapping of thrombin-receptor interactions
    • Y.M. Ayala, A.M. Cantwell, and T. Rose Molecular mapping of thrombin-receptor interactions Proteins 45 2001 107
    • (2001) Proteins , vol.45 , pp. 107
    • Ayala, Y.M.1    Cantwell, A.M.2    Rose, T.3
  • 47
    • 0035818425 scopus 로고    scopus 로고
    • Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib
    • R. De Cristofaro, E. De Candia, and R. Landolfi Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib Biochemistry 40 2001 13268
    • (2001) Biochemistry , vol.40 , pp. 13268
    • De Cristofaro, R.1    De Candia, E.2    Landolfi, R.3
  • 48
    • 0242384136 scopus 로고    scopus 로고
    • Targeting thrombin-rational drug design from natural mechanisms
    • J.A. Huntington, and T.P. Baglin Targeting thrombin-rational drug design from natural mechanisms Trends Pharmacol. Sci. 24 2003 589
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 589
    • Huntington, J.A.1    Baglin, T.P.2
  • 49
    • 0037143655 scopus 로고    scopus 로고
    • Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
    • T.P. Baglin, R.W. Carrell, and F.C. Church Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism Proc. Natl. Acad. Sci. U. S. A. 99 2002 11079
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11079
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3
  • 50
    • 11244267323 scopus 로고    scopus 로고
    • The staphylocoagulase family of zymogen activator and adhesion proteins
    • P. Panizzi, R. Friedrich, and P. Fuentes-Prior The staphylocoagulase family of zymogen activator and adhesion proteins Cell. Mol. Life Sci. 61 2004 2793
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2793
    • Panizzi, P.1    Friedrich, R.2    Fuentes-Prior, P.3
  • 51
    • 0141929350 scopus 로고    scopus 로고
    • Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation
    • R. Friedrich, P. Panizzi, and P. Fuentes-Prior Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation Nature 425 2003 535
    • (2003) Nature , vol.425 , pp. 535
    • Friedrich, R.1    Panizzi, P.2    Fuentes-Prior, P.3
  • 52
    • 33644866813 scopus 로고    scopus 로고
    • Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation
    • R. Friedrich, P. Panizzi, and S. Kawabata Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation JBC 281 2006 1188
    • (2006) JBC , vol.281 , pp. 1188
    • Friedrich, R.1    Panizzi, P.2    Kawabata, S.3
  • 53
    • 33644858159 scopus 로고    scopus 로고
    • Fibrinogen substrate recognition by staphylocoagulase•(pro)thrombin complexes
    • P. Panizzi, R. Friedrich, and P. Fuentes-Prior Fibrinogen substrate recognition by staphylocoagulase•(pro)thrombin complexes JBC 281 2006 1179
    • (2006) JBC , vol.281 , pp. 1179
    • Panizzi, P.1    Friedrich, R.2    Fuentes-Prior, P.3
  • 54
    • 0024464072 scopus 로고
    • Structural and functional properties of human alpha-thrombin, phosphopyridoxylated alpha-thrombin, and gamma T-thrombin. Identification of lysyl residues in alpha-thrombin that are critical for heparin and fibrin(ogen) interactions
    • F.C. Church, C.W. Pratt, and C.M. Noyes Structural and functional properties of human alpha-thrombin, phosphopyridoxylated alpha-thrombin, and gamma T-thrombin. Identification of lysyl residues in alpha-thrombin that are critical for heparin and fibrin(ogen) interactions J. Biol. Chem. 264 1989 18419
    • (1989) J. Biol. Chem. , vol.264 , pp. 18419
    • Church, F.C.1    Pratt, C.W.2    Noyes, C.M.3
  • 55
    • 0027972583 scopus 로고
    • Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III
    • Z.R. Gan, Y. Li, and Z. Chen Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III J. Biol. Chem. 269 1994 1301
    • (1994) J. Biol. Chem. , vol.269 , pp. 1301
    • Gan, Z.R.1    Li, Y.2    Chen, Z.3
  • 56
    • 13244270050 scopus 로고    scopus 로고
    • Crystal structure of thrombin bound to heparin
    • W.J. Carter, E. Cama, and J.A. Huntington Crystal structure of thrombin bound to heparin J. Biol. Chem. 280 2005 2745
    • (2005) J. Biol. Chem. , vol.280 , pp. 2745
    • Carter, W.J.1    Cama, E.2    Huntington, J.A.3
  • 57
    • 0025730441 scopus 로고    scopus 로고
    • Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models
    • S.T. Olson, H.R. Halvorson, and I. Bjork Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models J. Biol. Chem. 266 1991 6342
    • (1991) J. Biol. Chem. , vol.266 , pp. 6342
    • Olson, S.T.1    Halvorson, H.R.2    Bjork, I.3
  • 58
    • 0024456056 scopus 로고
    • Anti-thrombin activities of heparin. Effect of saccharide chain length on thrombin inhibition by heparin cofactor II and by antithrombin
    • B. Bray, D.A. Lane, and J.M. Freyssinet Anti-thrombin activities of heparin. Effect of saccharide chain length on thrombin inhibition by heparin cofactor II and by antithrombin Biochem. J. 262 1989 225
    • (1989) Biochem. J. , vol.262 , pp. 225
    • Bray, B.1    Lane, D.A.2    Freyssinet, J.M.3
  • 59
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • P.G. Gettins Serpin structure, mechanism, and function Chem. Rev. 102 2002 4751
    • (2002) Chem. Rev. , vol.102 , pp. 4751
    • Gettins, P.G.1
  • 60
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin
    • W. Li, D.J. Johnson, C.T. Esmon, and J.A. Huntington Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin Nat. Struct. Mol. Biol. 11 2004 857
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 857
    • Li, W.1    Johnson, D.J.2    Esmon, C.T.3    Huntington, J.A.4
  • 61
    • 4344710558 scopus 로고    scopus 로고
    • The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity
    • A. Dementiev, M. Petitou, J.M. Herbert, and P.G. Gettins The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity Nat. Struct. Mol. Biol. 11 2004 863
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 863
    • Dementiev, A.1    Petitou, M.2    Herbert, J.M.3    Gettins, P.G.4
  • 62
    • 0028332939 scopus 로고
    • Molecular mapping of the heparin-binding exosite of thrombin
    • J.P. Sheehan, and J.E. Sadler Molecular mapping of the heparin-binding exosite of thrombin Proc. Natl. Acad. Sci. U. S. A. 91 1994 5518
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5518
    • Sheehan, J.P.1    Sadler, J.E.2
  • 63
    • 0025730441 scopus 로고    scopus 로고
    • Quantitative characterization of the thrombin-heparin interaction
    • S.T. Olson Quantitative characterization of the thrombin-heparin interaction J. Biol. Chem. 266 1999 6342
    • (1999) J. Biol. Chem. , vol.266 , pp. 6342
    • Olson, S.T.1
  • 64
    • 0027288125 scopus 로고
    • Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin
    • R.K. Arni, K. Padmanabhan, and K.P. Padmanabhan Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin Biochemistry 32 1993 4727
    • (1993) Biochemistry , vol.32 , pp. 4727
    • Arni, R.K.1    Padmanabhan, K.2    Padmanabhan, K.P.3
  • 65
    • 0031574020 scopus 로고    scopus 로고
    • New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK
    • P.D. Martin, M.G. Malkowski, and J. Box New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK Structure 5 1997 1681
    • (1997) Structure , vol.5 , pp. 1681
    • Martin, P.D.1    Malkowski, M.G.2    Box, J.3
  • 66
    • 0034329465 scopus 로고    scopus 로고
    • Crystal structure of the human alpha-thrombin-haemadin complex: An exosite II-binding inhibitor
    • J.L. Richardson, B. Kröger, and W. Hoeffken Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor EMBO J. 19 2000 5650
    • (2000) EMBO J. , vol.19 , pp. 5650
    • Richardson, J.L.1    Kröger, B.2    Hoeffken, W.3
  • 67
    • 0037176829 scopus 로고    scopus 로고
    • Characterization of the residues involved in the human alpha-thrombin-haemadin complex: An exosite II-binding inhibitor
    • J.L. Richardson, P. Fuentes-Prior, and J.E. Sadler Characterization of the residues involved in the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor Biochemistry 41 2002 2535
    • (2002) Biochemistry , vol.41 , pp. 2535
    • Richardson, J.L.1    Fuentes-Prior, P.2    Sadler, J.E.3
  • 68
    • 0035852682 scopus 로고    scopus 로고
    • A thrombin receptor function for platelet glyco protein Ib-IX unmasked by cleavage of glycoprotein V
    • V. Ramakrishnan, F. DeGuzman, and M. Bao A thrombin receptor function for platelet glyco protein Ib-IX unmasked by cleavage of glycoprotein V Proc. Natl. Acad. Sci. U. S. A. 98 2001 1823
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1823
    • Ramakrishnan, V.1    Deguzman, F.2    Bao, M.3
  • 69
    • 0035877749 scopus 로고    scopus 로고
    • Unique pathway of thrombin-induced platelet aggregation mediated by glycoprotein Ib
    • G. Soslau, R. Class, and D.A. Morgan Unique pathway of thrombin-induced platelet aggregation mediated by glycoprotein Ib J. Biol. Chem. 276 2001 21173
    • (2001) J. Biol. Chem. , vol.276 , pp. 21173
    • Soslau, G.1    Class, R.2    Morgan, D.A.3
  • 70
    • 0742287058 scopus 로고    scopus 로고
    • The GPIbalpha-thrombin interaction: Far from crystal clear
    • K. Vanhoorelbeke, H. Ulrichts, and R.A. Romijn The GPIbalpha-thrombin interaction: far from crystal clear Trends Mol. Med. 10 2004 33
    • (2004) Trends Mol. Med. , vol.10 , pp. 33
    • Vanhoorelbeke, K.1    Ulrichts, H.2    Romijn, R.A.3
  • 71
    • 0038157329 scopus 로고    scopus 로고
    • Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation
    • J.J. Dumas, R. Kumar, and J. Seehra Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation Science 301 2003 222
    • (2003) Science , vol.301 , pp. 222
    • Dumas, J.J.1    Kumar, R.2    Seehra, J.3
  • 72
    • 0037815126 scopus 로고    scopus 로고
    • Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha
    • R. Celikel, R.A. McClintock, and J.R. Roberts Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha Science 301 2003 218
    • (2003) Science , vol.301 , pp. 218
    • Celikel, R.1    McClintock, R.A.2    Roberts, J.R.3
  • 73
    • 2942669901 scopus 로고    scopus 로고
    • The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function
    • T.E. Adams, M.F. Hockin, K.G. Mann, and S.J. Everse The crystal structure of activated protein C-inactivated bovine factor Va: implications for cofactor function Proc. Natl. Acad. Sci. U. S. A. 101 2004 8918
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8918
    • Adams, T.E.1    Hockin, M.F.2    Mann, K.G.3    Everse, S.J.4
  • 74
    • 1042276751 scopus 로고    scopus 로고
    • Activation of factor VIII and mechanisms of cofactor action
    • P.J. Fay Activation of factor VIII and mechanisms of cofactor action Blood Rev. 18 2004 1
    • (2004) Blood Rev. , vol.18 , pp. 1
    • Fay, P.J.1
  • 75
    • 0029935853 scopus 로고    scopus 로고
    • Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII
    • C.T. Esmon, and P. Lollar Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII J. Biol. Chem. 271 1996 13882
    • (1996) J. Biol. Chem. , vol.271 , pp. 13882
    • Esmon, C.T.1    Lollar, P.2
  • 76
    • 0035816595 scopus 로고    scopus 로고
    • An extensive interaction interface between thrombin and factor V is required for factor V activation
    • T. Myles, T.H. Yun, S.W. Hall, and L.L. Leung An extensive interaction interface between thrombin and factor V is required for factor V activation J. Biol. Chem. 276 2001 25143
    • (2001) J. Biol. Chem. , vol.276 , pp. 25143
    • Myles, T.1    Yun, T.H.2    Hall, S.W.3    Leung, L.L.4
  • 77
    • 0037108447 scopus 로고    scopus 로고
    • Structural requirements for the activation of human factor VIII by thrombin
    • T. Myles, T.H. Yun, and L.L. Leung Structural requirements for the activation of human factor VIII by thrombin Blood 100 2002 2820
    • (2002) Blood , vol.100 , pp. 2820
    • Myles, T.1    Yun, T.H.2    Leung, L.L.3
  • 78
    • 1842840779 scopus 로고    scopus 로고
    • Roles of factor XI, platelets and tissue factor-initiated blood coagulation
    • P.N. Walsh Roles of factor XI, platelets and tissue factor-initiated blood coagulation J. Thromb. Haemost. 1 2003 2081
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2081
    • Walsh, P.N.1
  • 79
    • 0030067448 scopus 로고    scopus 로고
    • A binding site for thrombin in the apple 1 domain of factor XI
    • F.A. Baglia, and P.N. Walsh A binding site for thrombin in the apple 1 domain of factor XI J. Biol. Chem. 271 1996 3652
    • (1996) J. Biol. Chem. , vol.271 , pp. 3652
    • Baglia, F.A.1    Walsh, P.N.2
  • 80
    • 0346850827 scopus 로고    scopus 로고
    • Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively
    • T.H. Yun, F.A. Baglia, and T. Myles Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively J. Biol. Chem. 278 2003 48112
    • (2003) J. Biol. Chem. , vol.278 , pp. 48112
    • Yun, T.H.1    Baglia, F.A.2    Myles, T.3
  • 81
    • 0029112841 scopus 로고
    • Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface
    • C.T. Esmon Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface FASEB J. 9 1995 946
    • (1995) FASEB J. , vol.9 , pp. 946
    • Esmon, C.T.1
  • 82
    • 0034732094 scopus 로고    scopus 로고
    • Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex
    • P. Fuentes-Prior, Y. Iwanaga, and R. Huber Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex Nature 404 2000 518
    • (2000) Nature , vol.404 , pp. 518
    • Fuentes-Prior, P.1    Iwanaga, Y.2    Huber, R.3
  • 83
    • 0034725622 scopus 로고    scopus 로고
    • Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation
    • W. Wang, M. Nagashima, and M. Schneider Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation J. Biol. Chem. 275 2000 22942
    • (2000) J. Biol. Chem. , vol.275 , pp. 22942
    • Wang, W.1    Nagashima, M.2    Schneider, M.3
  • 84
    • 0034006172 scopus 로고    scopus 로고
    • Solution structure of the smallest cofactor-active fragment of thrombomodulin
    • M.J. Wood, B.A. Sampoli Benitez, and E.A. Komives Solution structure of the smallest cofactor-active fragment of thrombomodulin Nat. Struct. Biol. 7 2000 200
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 200
    • Wood, M.J.1    Sampoli Benitez, B.A.2    Komives, E.A.3
  • 85
    • 0028338559 scopus 로고
    • Glycosaminoglycan contributions to both protein C activation and thrombin inhibition involve a common arginine-rich site in thrombin that includes residues arginine 93, 97, and 101
    • J. Ye, A.R. Rezaie, and C.T. Esmon Glycosaminoglycan contributions to both protein C activation and thrombin inhibition involve a common arginine-rich site in thrombin that includes residues arginine 93, 97, and 101 J. Biol. Chem. 269 1994 17965
    • (1994) J. Biol. Chem. , vol.269 , pp. 17965
    • Ye, J.1    Rezaie, A.R.2    Esmon, C.T.3
  • 86
    • 0027411150 scopus 로고
    • Alanine-scanning mutagenesis of the epidermal growth factor-like domains of human thrombomodulin identifies critical residues for its cofactor activity
    • M. Nagashima, E. Lundh, and J.C. Leonard Alanine-scanning mutagenesis of the epidermal growth factor-like domains of human thrombomodulin identifies critical residues for its cofactor activity J. Biol. Chem. 268 1993 2888
    • (1993) J. Biol. Chem. , vol.268 , pp. 2888
    • Nagashima, M.1    Lundh, E.2    Leonard, J.C.3
  • 87
    • 0030468098 scopus 로고    scopus 로고
    • The 2.8 a crystal structure of Gla-domainless activated protein C
    • T. Mather, V. Oganessyan, and P. Hof The 2.8 A crystal structure of Gla-domainless activated protein C EMBO J. 15 1996 6822
    • (1996) EMBO J. , vol.15 , pp. 6822
    • Mather, T.1    Oganessyan, V.2    Hof, P.3
  • 88
    • 0029787653 scopus 로고    scopus 로고
    • Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin
    • B. Gerlitz, and B.W. Grinnell Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin J. Biol. Chem. 271 1996 22285
    • (1996) J. Biol. Chem. , vol.271 , pp. 22285
    • Gerlitz, B.1    Grinnell, B.W.2
  • 89
    • 0029000452 scopus 로고
    • Amino acids 225-235** of the protein C serine-protease domain are important for the interaction with the thrombin-thrombomodulin complex
    • A. Vincenot, P. Gaussem, and J.L. Pittet Amino acids 225-235** of the protein C serine-protease domain are important for the interaction with the thrombin-thrombomodulin complex FEBS Lett. 367 1995 153
    • (1995) FEBS Lett. , vol.367 , pp. 153
    • Vincenot, A.1    Gaussem, P.2    Pittet, J.L.3
  • 90
    • 0037518132 scopus 로고    scopus 로고
    • The fourth epidermal growth factor-like domain of thrombomodulin interacts with the basic exosite of protein C
    • L. Yang, and A.R. Rezaie The fourth epidermal growth factor-like domain of thrombomodulin interacts with the basic exosite of protein C J. Biol. Chem. 278 2003 10484 10490
    • (2003) J. Biol. Chem. , vol.278 , pp. 10484-10490
    • Yang, L.1    Rezaie, A.R.2
  • 91
    • 14844331743 scopus 로고    scopus 로고
    • Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C
    • H. Xu, L.A. Bush, and A.O. Pineda Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C J. Biol. Chem. 280 2005 7956
    • (2005) J. Biol. Chem. , vol.280 , pp. 7956
    • Xu, H.1    Bush, L.A.2    Pineda, A.O.3
  • 92
    • 24344495389 scopus 로고    scopus 로고
    • Mutagenesis studies toward understanding the mechanism of the cofactor function of thrombomodulin
    • A.R. Rezaie, and L. Yang Mutagenesis studies toward understanding the mechanism of the cofactor function of thrombomodulin Biophys. Chem. 117 2005 255
    • (2005) Biophys. Chem. , vol.117 , pp. 255
    • Rezaie, A.R.1    Yang, L.2
  • 93
    • 17644420041 scopus 로고    scopus 로고
    • The affinity of protein C for the thrombin.thrombomodulin complex is determined in a primary way by active site-dependent interactions
    • G. Lu, S. Chhum, and S. Krishnaswamy The affinity of protein C for the thrombin.thrombomodulin complex is determined in a primary way by active site-dependent interactions J. Biol. Chem. 280 2005 15471
    • (2005) J. Biol. Chem. , vol.280 , pp. 15471
    • Lu, G.1    Chhum, S.2    Krishnaswamy, S.3
  • 94
    • 0141484541 scopus 로고    scopus 로고
    • Thrombin interactions
    • E. Di Cera Thrombin interactions CHEST 124 2003 1S
    • (2003) CHEST , vol.124
    • Di Cera, E.1
  • 95
    • 0025977159 scopus 로고
    • Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its inactivity
    • M. Coll, A. Guasch, F.X. Aviles, and R. Huber Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity EMBO J. 10 1991 1
    • (1991) EMBO J. , vol.10 , pp. 1
    • Coll, M.1    Guasch, A.2    Aviles, F.X.3    Huber, R.4
  • 96
    • 0037155855 scopus 로고    scopus 로고
    • Amino acid residues in the P6-P′3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation
    • M. Schneider, M. Nagashima, and S. Knappe Amino acid residues in the P6-P′3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation J. Biol. Chem. 277 2002 9944
    • (2002) J. Biol. Chem. , vol.277 , pp. 9944
    • Schneider, M.1    Nagashima, M.2    Knappe, S.3
  • 97
    • 0034083954 scopus 로고    scopus 로고
    • The plot thickens: How thrombin modulates blood clotting
    • M. Overduin, and T. de Beer The plot thickens: how thrombin modulates blood clotting Nat. Struct. Biol. 7 2000 267
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 267
    • Overduin, M.1    De Beer, T.2
  • 98
    • 28044444092 scopus 로고    scopus 로고
    • The structure of thrombin, a chameleon-like proteinase
    • W. Bode The structure of thrombin, a chameleon-like proteinase J. Thromb. Haemost. 3 2005 2379
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 2379
    • Bode, W.1


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