메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

On the Specificity of Heparin/Heparan Sulfate Binding to Proteins. Anion-Binding Sites on Antithrombin and Thrombin Are Fundamentally Different

Author keywords

[No Author keywords available]

Indexed keywords

ANION; ANTITHROMBIN; ARGININE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; LYSINE; PENTASACCHARIDE; SOLVENT; THROMBIN; WATER;

EID: 84869073602     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0048632     Document Type: Article
Times cited : (48)

References (59)
  • 2
    • 15244364003 scopus 로고    scopus 로고
    • Heparan sulfate-protein interactions: therapeutic potential through structure-function insights
    • Coombe DR, Kett WC, (2005) Heparan sulfate-protein interactions: therapeutic potential through structure-function insights. Cell Mol Life Sci 62: 410-424.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 410-424
    • Coombe, D.R.1    Kett, W.C.2
  • 3
    • 56649100319 scopus 로고    scopus 로고
    • The structure of glycosaminoglycans and their interactions with proteins
    • Gandhi NS, Mancera RL, (2008) The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des 72: 455-482.
    • (2008) Chem Biol Drug Des , vol.72 , pp. 455-482
    • Gandhi, N.S.1    Mancera, R.L.2
  • 4
    • 15744403559 scopus 로고    scopus 로고
    • Structural insights into biological roles of protein-glycosaminoglycan interactions
    • Raman R, Sasisekharan V, Sasisekharan R, (2005) Structural insights into biological roles of protein-glycosaminoglycan interactions. Chem Biol 12: 267-277.
    • (2005) Chem Biol , vol.12 , pp. 267-277
    • Raman, R.1    Sasisekharan, V.2    Sasisekharan, R.3
  • 6
    • 77958189486 scopus 로고    scopus 로고
    • Glycosaminoglycan (GAG) Biosynthesis and GAG-binding proteins
    • Zhang L, (2010) Glycosaminoglycan (GAG) Biosynthesis and GAG-binding proteins. Prog Mol Biol Transl Sci 93: 1-17.
    • (2010) Prog Mol Biol Transl Sci , vol.93 , pp. 1-17
    • Zhang, L.1
  • 7
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: assembly of ligand binding sites in heparan sulfate
    • Esko JD, Selleck SB, (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 71: 435-471.
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 8
    • 0033650826 scopus 로고    scopus 로고
    • Conformation and dynamics of heparin and heparan sulfate
    • Mulloy B, Forster MJ, (2000) Conformation and dynamics of heparin and heparan sulfate. Glycobiology 10: 1147-1156.
    • (2000) Glycobiology , vol.10 , pp. 1147-1156
    • Mulloy, B.1    Forster, M.J.2
  • 9
    • 0032571333 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin. Role of individual residues of the pentasaccharide activating sequence in the recognition of native and activated states of antithrombin
    • Desai UR, Petitou M, Björk I, Olson ST, (1998) Mechanism of heparin activation of antithrombin. Role of individual residues of the pentasaccharide activating sequence in the recognition of native and activated states of antithrombin. J Biol Chem 273: 7478-7487.
    • (1998) J Biol Chem , vol.273 , pp. 7478-7487
    • Desai, U.R.1    Petitou, M.2    Björk, I.3    Olson, S.T.4
  • 11
    • 44349157970 scopus 로고    scopus 로고
    • Using a 3-O-sulfated heparin octasaccharide to inhibit the entry of herpes simplex virus type 1
    • Copeland R, Balasubramaniam A, Tiwari V, Zhang F, Bridges A, et al. (2008) Using a 3-O-sulfated heparin octasaccharide to inhibit the entry of herpes simplex virus type 1. Biochemistry 47: 5774-5783.
    • (2008) Biochemistry , vol.47 , pp. 5774-5783
    • Copeland, R.1    Balasubramaniam, A.2    Tiwari, V.3    Zhang, F.4    Bridges, A.5
  • 12
    • 0037031877 scopus 로고    scopus 로고
    • Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D
    • Liu J, Shriver Z, Pope RM, Thorpe SC, Duncan MB, et al. (2002) Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D. J Biol Chem 277: 33456-33467.
    • (2002) J Biol Chem , vol.277 , pp. 33456-33467
    • Liu, J.1    Shriver, Z.2    Pope, R.M.3    Thorpe, S.C.4    Duncan, M.B.5
  • 13
    • 69749127705 scopus 로고    scopus 로고
    • Compositional analysis of heparin/heparan sulfate interacting with fibroblast growth factor • fibroblast growth factor receptor complexes
    • Zhang F, Zhang Z, Lin X, Beenken A, Eliseenkova AV, et al. (2009) Compositional analysis of heparin/heparan sulfate interacting with fibroblast growth factor • fibroblast growth factor receptor complexes. Biochemistry 48: 8379-8386.
    • (2009) Biochemistry , vol.48 , pp. 8379-8386
    • Zhang, F.1    Zhang, Z.2    Lin, X.3    Beenken, A.4    Eliseenkova, A.V.5
  • 14
    • 1842530198 scopus 로고    scopus 로고
    • Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library
    • Ashikari-Hada S, Habuchi H, Kariya Y, Itoh N, Reddi AH, et al. (2004) Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library. J Biol Chem 279: 12346-12354.
    • (2004) J Biol Chem , vol.279 , pp. 12346-12354
    • Ashikari-Hada, S.1    Habuchi, H.2    Kariya, Y.3    Itoh, N.4    Reddi, A.H.5
  • 16
    • 0034696765 scopus 로고    scopus 로고
    • Consequences of the non-specific binding of a protein to a linear polymer: reconciliation of stoichiometric and equilibrium titration data for the thrombin-heparin interaction
    • Munro PD, Jackson CM, Winzor DJ, (2000) Consequences of the non-specific binding of a protein to a linear polymer: reconciliation of stoichiometric and equilibrium titration data for the thrombin-heparin interaction. J Theor Biol 203: 407-418.
    • (2000) J Theor Biol , vol.203 , pp. 407-418
    • Munro, P.D.1    Jackson, C.M.2    Winzor, D.J.3
  • 17
    • 0025730441 scopus 로고
    • Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models
    • Olson ST, Halvorson HR, Björk 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    Björk, I.3
  • 19
    • 73249126308 scopus 로고    scopus 로고
    • Synergistic effect of aptamers that inhibit exosites 1 and 2 on thrombin
    • Nimjee SM, Oney S, Volovyk Z, Bompiani KM, Long SB, et al. (2009) Synergistic effect of aptamers that inhibit exosites 1 and 2 on thrombin. RNA 15: 2105-2111.
    • (2009) RNA , vol.15 , pp. 2105-2111
    • Nimjee, S.M.1    Oney, S.2    Volovyk, Z.3    Bompiani, K.M.4    Long, S.B.5
  • 20
    • 13244270050 scopus 로고    scopus 로고
    • Crystal structure of thrombin bound to heparin
    • Carter WJ, Cama E, Huntington JA, (2005) Crystal structure of thrombin bound to heparin. J Biol Chem 280: 2745-2749.
    • (2005) J Biol Chem , vol.280 , pp. 2745-2749
    • Carter, W.J.1    Cama, E.2    Huntington, J.A.3
  • 21
    • 34548046764 scopus 로고    scopus 로고
    • Glycosaminoglycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers
    • Abzalimov RR, Dubin PL, Kaltashov IA, (2007) Glycosaminoglycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers. Anal Chem 79: 6055-6063.
    • (2007) Anal Chem , vol.79 , pp. 6055-6063
    • Abzalimov, R.R.1    Dubin, P.L.2    Kaltashov, I.A.3
  • 22
    • 77951684925 scopus 로고    scopus 로고
    • Screening for anticoagulant heparan sulfate octasaccharides and fine structure characterization using tandem mass spectrometry
    • Naimy H, Leymarie N, Zaia J, (2010) Screening for anticoagulant heparan sulfate octasaccharides and fine structure characterization using tandem mass spectrometry. Biochemistry 49: 3743-3752.
    • (2010) Biochemistry , vol.49 , pp. 3743-3752
    • Naimy, H.1    Leymarie, N.2    Zaia, J.3
  • 23
    • 33644946682 scopus 로고    scopus 로고
    • Microarrays of synthetic heparin oligosaccharides
    • de Paz JL, Noti C, Seeberger PH, (2006) Microarrays of synthetic heparin oligosaccharides. J Am Chem Soc 128: 2766-2767.
    • (2006) J Am Chem Soc , vol.128 , pp. 2766-2767
    • de Paz, J.L.1    Noti, C.2    Seeberger, P.H.3
  • 24
    • 53049110572 scopus 로고    scopus 로고
    • Signal amplification of target protein on heparin glycan microarray
    • Park TJ, Lee MY, Dordick JS, Linhardt RJ, (2008) Signal amplification of target protein on heparin glycan microarray. Anal Biochem 383: 116-121.
    • (2008) Anal Biochem , vol.383 , pp. 116-121
    • Park, T.J.1    Lee, M.Y.2    Dordick, J.S.3    Linhardt, R.J.4
  • 25
    • 33745119433 scopus 로고    scopus 로고
    • Finding a needle in a haystack: development of a combinatorial virtual screening approach for identifying high specificity heparin/heparan sulfate sequence(s)
    • Raghuraman A, Mosier PD, Desai UR, (2006) Finding a needle in a haystack: development of a combinatorial virtual screening approach for identifying high specificity heparin/heparan sulfate sequence(s). J Med Chem 49: 3553-3562.
    • (2006) J Med Chem , vol.49 , pp. 3553-3562
    • Raghuraman, A.1    Mosier, P.D.2    Desai, U.R.3
  • 27
    • 80051505598 scopus 로고    scopus 로고
    • Molecular modeling of the interaction between heparan sulfate and cellular growth factors: bringing the pieces together
    • Sapay N, Cabannes E, Petitou M, Imberty A, (2011) Molecular modeling of the interaction between heparan sulfate and cellular growth factors: bringing the pieces together. Glycobiology 21: 1181-1193.
    • (2011) Glycobiology , vol.21 , pp. 1181-1193
    • Sapay, N.1    Cabannes, E.2    Petitou, M.3    Imberty, A.4
  • 28
    • 79952156437 scopus 로고    scopus 로고
    • Molecular dynamics simulations of CXCL-8 and its interactions with a receptor peptide, heparin fragments, and sulfated linked cyclitols
    • Gandhi NS, Mancera RL, (2011) Molecular dynamics simulations of CXCL-8 and its interactions with a receptor peptide, heparin fragments, and sulfated linked cyclitols. J Chem Inf Model 51: 335-358.
    • (2011) J Chem Inf Model , vol.51 , pp. 335-358
    • Gandhi, N.S.1    Mancera, R.L.2
  • 29
  • 30
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins
    • Hileman RE, Fromm JR, Weiler JM, Linhardt RJ, (1998) Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins. Bioessays 20: 156-167.
    • (1998) Bioessays , vol.20 , pp. 156-167
    • Hileman, R.E.1    Fromm, J.R.2    Weiler, J.M.3    Linhardt, R.J.4
  • 31
    • 0027327277 scopus 로고
    • Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues
    • Margalit H, Fischer N, Ben-Sasson SA, (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J Biol Chem 268: 19228-19231.
    • (1993) J Biol Chem , vol.268 , pp. 19228-19231
    • Margalit, H.1    Fischer, N.2    Ben-Sasson, S.A.3
  • 32
    • 84864647179 scopus 로고    scopus 로고
    • The "CPC Clip Motif": A Conserved Structural Signature for Heparin-Binding Proteins
    • Torrent M, Nogués MV, Andreu D, Boix E, (2012) The "CPC Clip Motif": A Conserved Structural Signature for Heparin-Binding Proteins. PLoS One 7: e42692.
    • (2012) PLoS One , vol.7
    • Torrent, M.1    Nogués, M.V.2    Andreu, D.3    Boix, E.4
  • 33
    • 79957592466 scopus 로고    scopus 로고
    • A systems biology approach for the investigation of the heparin/heparan sulfate interactome
    • Ori A, Wilkinson MC, Fernig DG, (2011) A systems biology approach for the investigation of the heparin/heparan sulfate interactome. J Biol Chem 286: 19892-19904.
    • (2011) J Biol Chem , vol.286 , pp. 19892-19904
    • Ori, A.1    Wilkinson, M.C.2    Fernig, D.G.3
  • 34
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor
    • Fromm JR, Hileman RE, Caldwell EEO, Weiler JM, Linhardt RJ, (1995) Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor. Arch Biochem Biophys 323: 279-287.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.O.3    Weiler, J.M.4    Linhardt, R.J.5
  • 35
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the Antithrombin-Thrombin-Heparin Ternary Complex Reveals the Antithrombotic Mechanism of Heparin
    • Li W, Johnson DJD, Esmon CT, Huntington JA, (2004) Structure of the Antithrombin-Thrombin-Heparin Ternary Complex Reveals the Antithrombotic Mechanism of Heparin. Nat Struct Mol Biol 11: 857-862.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 857-862
    • Li, W.1    Johnson, D.J.D.2    Esmon, C.T.3    Huntington, J.A.4
  • 36
    • 0025357582 scopus 로고
    • Structural Refinement and Analysis of Mengo Virus
    • Krishnawamy S, Rossman MG, (1990) Structural Refinement and Analysis of Mengo Virus. J Mol Biol 211: 803-844.
    • (1990) J Mol Biol , vol.211 , pp. 803-844
    • Krishnawamy, S.1    Rossman, M.G.2
  • 37
    • 77949320406 scopus 로고    scopus 로고
    • A novel and efficient tool for locating and characterizing protein cavities and binding sites
    • Tripathi A, Kellogg GE, (2010) A novel and efficient tool for locating and characterizing protein cavities and binding sites. Proteins 78: 825-842.
    • (2010) Proteins , vol.78 , pp. 825-842
    • Tripathi, A.1    Kellogg, G.E.2
  • 38
    • 0343517556 scopus 로고    scopus 로고
    • Hydrophobicity: is logPo/w more than the sum of its parts?
    • Kellogg GE, Abraham DJ, (2000) Hydrophobicity: is logPo/w more than the sum of its parts? Eur J Med Chem 35: 651-661.
    • (2000) Eur J Med Chem , vol.35 , pp. 651-661
    • Kellogg, G.E.1    Abraham, D.J.2
  • 39
    • 33645941696 scopus 로고    scopus 로고
    • New application design for a 3d hydropathic map-based search for potential water molecules bridging between protein and ligand
    • Kellogg GE, Fornabaio M, Chen DL, Abraham DJ, (2005) New application design for a 3d hydropathic map-based search for potential water molecules bridging between protein and ligand. Internet Electron J Mol Des 4: 194-209.
    • (2005) Internet Electron J Mol Des , vol.4 , pp. 194-209
    • Kellogg, G.E.1    Fornabaio, M.2    Chen, D.L.3    Abraham, D.J.4
  • 40
    • 4143131457 scopus 로고    scopus 로고
    • The importance of being exhaustive. Optimization of bridging structural water molecules and water networks in models of biological systems
    • Kellogg GE, Chen DL, (2004) The importance of being exhaustive. Optimization of bridging structural water molecules and water networks in models of biological systems. Chem Biodivers 1: 98-105.
    • (2004) Chem Biodivers , vol.1 , pp. 98-105
    • Kellogg, G.E.1    Chen, D.L.2
  • 41
    • 39749105264 scopus 로고    scopus 로고
    • Robust classification of "Relevant" water molecules in putative protein binding sites
    • Amadasi A, Surface JA, Spyrakis F, Cozzini P, Mozzarelli A, et al. (2008) Robust classification of "Relevant" water molecules in putative protein binding sites. J Med Chem 51: 1063-1067.
    • (2008) J Med Chem , vol.51 , pp. 1063-1067
    • Amadasi, A.1    Surface, J.A.2    Spyrakis, F.3    Cozzini, P.4    Mozzarelli, A.5
  • 42
    • 4544280219 scopus 로고    scopus 로고
    • A synthetic antithrombin III binding pentasaccharide is now a drug! What comes next?
    • Petitou M, van Boeckel CAA, (2004) A synthetic antithrombin III binding pentasaccharide is now a drug! What comes next? Angew Chem Int Ed Engl 43: 3118-3133.
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 3118-3133
    • Petitou, M.1    van Boeckel, C.A.A.2
  • 43
    • 0030822767 scopus 로고    scopus 로고
    • Influence of arginines 93, 97, and 101 of thrombin to its functional specificity
    • He X, Ye J, Esmon CT, Rezaie AR, (1997) Influence of arginines 93, 97, and 101 of thrombin to its functional specificity. Biochemistry 36: 8969-8976.
    • (1997) Biochemistry , vol.36 , pp. 8969-8976
    • He, X.1    Ye, J.2    Esmon, C.T.3    Rezaie, A.R.4
  • 44
    • 0037108171 scopus 로고    scopus 로고
    • Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding
    • Schedin-Weiss S, Arocas V, Bock SC, Olson ST, Björk I, (2002) Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding. Biochemistry 41: 12369-12376.
    • (2002) Biochemistry , vol.41 , pp. 12369-12376
    • Schedin-Weiss, S.1    Arocas, V.2    Bock, S.C.3    Olson, S.T.4    Björk, I.5
  • 45
    • 0027918556 scopus 로고
    • Water: now you see it, now you don't
    • Levitt M, Park BH, (1993) Water: now you see it, now you don't. Structure 1: 223-226.
    • (1993) Structure , vol.1 , pp. 223-226
    • Levitt, M.1    Park, B.H.2
  • 46
    • 4143121554 scopus 로고    scopus 로고
    • Free energy of ligand binding to protein: evaluation of the contribution of water molecules by computational methods
    • Cozzini P, Fornabaio M, Marabotti A, Abraham DJ, Kellogg GE, et al. (2004) Free energy of ligand binding to protein: evaluation of the contribution of water molecules by computational methods. Curr Med Chem 11: 3093-3118.
    • (2004) Curr Med Chem , vol.11 , pp. 3093-3118
    • Cozzini, P.1    Fornabaio, M.2    Marabotti, A.3    Abraham, D.J.4    Kellogg, G.E.5
  • 47
    • 4344710558 scopus 로고    scopus 로고
    • The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor selectivity
    • Dementiev A, Petitou M, Herbert JM, Gettins PGW, (2004) The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor selectivity. Nat Struct Mol Biol 11: 863-867.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 863-867
    • Dementiev, A.1    Petitou, M.2    Herbert, J.M.3    Gettins, P.G.W.4
  • 48
    • 29144482496 scopus 로고    scopus 로고
    • Comprehensive identification of "druggable" protein ligand binding sites
    • An J, Totrov M, Abagyan R, (2004) Comprehensive identification of "druggable" protein ligand binding sites. Genome Inform 15: 31-41.
    • (2004) Genome Inform , vol.15 , pp. 31-41
    • An, J.1    Totrov, M.2    Abagyan, R.3
  • 49
    • 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
    • Ye J, Rezaie AR, Esmon CT, (1994) 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: 17965-17970.
    • (1994) J Biol Chem , vol.269 , pp. 17965-17970
    • Ye, J.1    Rezaie, A.R.2    Esmon, C.T.3
  • 51
    • 79952174904 scopus 로고    scopus 로고
    • Proteins that Bind Sulfated Glycosaminoglycans
    • Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, editors, Cold Spring Harbor, New York, Cold Spring Harbor Laboratory Press
    • Esko JD, Linhardt RJ (2009) Proteins that Bind Sulfated Glycosaminoglycans. In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, editors. Essentials of Glycobiology, 2nd Ed., Cold Spring Harbor, New York, Cold Spring Harbor Laboratory Press. pp. 501-511.
    • (2009) Essentials of Glycobiology , pp. 501-511
    • Esko, J.D.1    Linhardt, R.J.2
  • 52
    • 42449150052 scopus 로고    scopus 로고
    • Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-Å structure of the heparin-bridged complex
    • Li W, Adams TE, Nangalia J, Esmon CT, Huntington JA, (2008) Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-Å structure of the heparin-bridged complex. Proc Natl Acad Sci U S A 105: 4661-4666.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4661-4666
    • Li, W.1    Adams, T.E.2    Nangalia, J.3    Esmon, C.T.4    Huntington, J.A.5
  • 53
    • 0034329465 scopus 로고    scopus 로고
    • Crystal Structure of the Human α-Thrombin-Haemadin Complex: An Exosite II-binding Inhibitor
    • Richardson JL, Kröger B, Hoeffken W, Sadler JE, Pereira P, et al. (2000) Crystal Structure of the Human α-Thrombin-Haemadin Complex: An Exosite II-binding Inhibitor. EMBO J 19: 5650-5660.
    • (2000) EMBO J , vol.19 , pp. 5650-5660
    • Richardson, J.L.1    Kröger, B.2    Hoeffken, W.3    Sadler, J.E.4    Pereira, P.5
  • 54
    • 0037143655 scopus 로고    scopus 로고
    • Crystal Structures of Native and Thrombin-Complexed Heparin Cofactor II Reveal a Multistep Allosteric Mechanism
    • Baglin TP, Carrell RW, Church FC, Esmon CT, Huntington JA, (2002) Crystal Structures of Native and Thrombin-Complexed Heparin Cofactor II Reveal a Multistep Allosteric Mechanism. Proc Natl Acad Sci U S A 99: 11079-11084.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11079-11084
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3    Esmon, C.T.4    Huntington, J.A.5
  • 55
    • 33845955477 scopus 로고    scopus 로고
    • Crystal Structure of Monomeric Native Antithrombin Reveals a Novel Reactive Center Loop Conformation
    • Johnson DJD, Langdown J, Li W, Luis SA, Baglin TP, et al. (2006) Crystal Structure of Monomeric Native Antithrombin Reveals a Novel Reactive Center Loop Conformation. J Biol Chem 281: 35478-35486.
    • (2006) J Biol Chem , vol.281 , pp. 35478-35486
    • Johnson, D.J.D.1    Langdown, J.2    Li, W.3    Luis, S.A.4    Baglin, T.P.5
  • 56
    • 0037459052 scopus 로고    scopus 로고
    • Structure of β-Antithrombin and the Effect of Glycosylation on Antithrombin's Heparin Affinity and Activity
    • McCoy AJ, Pei XY, Skinner R, Abrahams JP, Carrell RW, (2003) Structure of β-Antithrombin and the Effect of Glycosylation on Antithrombin's Heparin Affinity and Activity. J Mol Biol 326: 823-833.
    • (2003) J Mol Biol , vol.326 , pp. 823-833
    • McCoy, A.J.1    Pei, X.Y.2    Skinner, R.3    Abrahams, J.P.4    Carrell, R.W.5
  • 57
    • 0041846670 scopus 로고    scopus 로고
    • Crystal Structure of Antithrombin in a Heparin-Bound Intermediate State
    • Johnson DJD, Huntington JA, (2003) Crystal Structure of Antithrombin in a Heparin-Bound Intermediate State. Biochemistry 42: 8712-8719.
    • (2003) Biochemistry , vol.42 , pp. 8712-8719
    • Johnson, D.J.D.1    Huntington, J.A.2
  • 58
    • 33646581724 scopus 로고    scopus 로고
    • Antithrombin-S195A Factor Xa-Heparin Structure Reveals the Allosteric Mechanism of Antithrombin Activation
    • Johnson DJD, Li W, Adams TE, Huntington JA, (2006) Antithrombin-S195A Factor Xa-Heparin Structure Reveals the Allosteric Mechanism of Antithrombin Activation. EMBO J 25: 2029-2037.
    • (2006) EMBO J , vol.25 , pp. 2029-2037
    • Johnson, D.J.D.1    Li, W.2    Adams, T.E.3    Huntington, J.A.4
  • 59
    • 60849096635 scopus 로고    scopus 로고
    • The Critical Role of Hinge-Region Expulsion in the Induced-Fit Heparin Binding Mechanism of Antithrombin
    • Langdown J, Belzar KJ, Savory WJ, Baglin TP, Huntington JA, (2009) The Critical Role of Hinge-Region Expulsion in the Induced-Fit Heparin Binding Mechanism of Antithrombin. J Mol Biol 386: 1278-1289.
    • (2009) J Mol Biol , vol.386 , pp. 1278-1289
    • Langdown, J.1    Belzar, K.J.2    Savory, W.J.3    Baglin, T.P.4    Huntington, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.