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Volumn 41, Issue 12, 1998, Pages 2068-2075

Structural analysis of thrombin complexed with potent inhibitors incorporating a phenyl group as a peptide mimetic and aminopyridines as guanidine substitutes

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOPYRIDINE DERIVATIVE; CARBONYL DERIVATIVE; FIBRINOGEN RECEPTOR ANTAGONIST; GUANIDINE DERIVATIVE; HIRUDIN; PHENYL GROUP; PROTEIN FARNESYLTRANSFERASE INHIBITOR; SOLVENT; THROMBIN; THROMBIN INHIBITOR;

EID: 0032482311     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm970796l     Document Type: Article
Times cited : (28)

References (49)
  • 3
    • 0030046735 scopus 로고    scopus 로고
    • Design and Synthesis of Non- Peptide Ras CAAX Mimetics as Potent Farnesyltransferase Inhibitors
    • Qian, Y.; Vogt, A.; Sebti, S. M.; Hamilton, A. D. Design and Synthesis of Non- Peptide Ras CAAX Mimetics as Potent Farnesyltransferase Inhibitors. J. Med Chem. 1996, 39, 217- 223.
    • (1996) J. Med Chem. , vol.39 , pp. 217-223
    • Qian, Y.1    Vogt, A.2    Sebti, S.M.3    Hamilton, A.D.4
  • 4
    • 0028132044 scopus 로고
    • Peptidomimetic Inhibitors of P21Ras Farnesyltransferase: Hydrophobic Functionalization Leads to Disruption of P21Ras Membrane Association in Whole Cells
    • Qian Y.; Blaskovich, M. A.; Seong, C. M.; Vogt, A.; Hamilton, A. D.; Sebti, S. M. Peptidomimetic Inhibitors of P21Ras Farnesyltransferase: Hydrophobic Functionalization Leads to Disruption of P21Ras Membrane Association in Whole Cells. Bioog. Med. Chem. Lett. 1994, 4, 2579-2584.
    • (1994) Bioog. Med. Chem. Lett. , vol.4 , pp. 2579-2584
    • Qian, Y.1    Blaskovich, M.A.2    Seong, C.M.3    Vogt, A.4    Hamilton, A.D.5    Sebti, S.M.6
  • 8
    • 0030895222 scopus 로고    scopus 로고
    • Design of Highly Potent Noncovalent Thrombin Inhibitors That Utilize a Novel Lipophilic Binding Pocket in the Thrombin Active Site
    • Tucker, T. J.; Lumma, W. C.; Mulichak, A. M.; Chen, Z.; Naylor- Olsen, A. M.; Lewis, S. D.; Lucas, R.; Freidinger, R. M.; Kuo, L. C. Design of Highly Potent Noncovalent Thrombin Inhibitors That Utilize a Novel Lipophilic Binding Pocket in the Thrombin Active Site. J. Med. Chem. 1997, 40, 830-832.
    • (1997) J. Med. Chem. , vol.40 , pp. 830-832
    • Tucker, T.J.1    Lumma, W.C.2    Mulichak, A.M.3    Chen, Z.4    Olsen, A.M.5    Lewis, S.D.6    Lucas, R.7    Freidinger, R.M.8    Kuo, L.C.9
  • 11
    • 0014211618 scopus 로고
    • On the Size of the Active site in Proteases. I. Papain
    • Schechter, I.; Berger, A. On the Size of the Active site in Proteases. I. Papain. Biochem. Biophys. Res. Commun. 1967, 27, 157.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157
    • Schechter, I.1    Berger, A.2
  • 12
    • 0028930160 scopus 로고
    • Kinetic and Crystallographic Studies of Thrombin with Ac-(D)Phe-Pro-boroArg-OH and Its Lysine, Amidine, Homolysine and Ornithine Analogs
    • Webber, P. C.; Lee, S.-L.; Lewandowski, F. A.; Schadt, M. C.; Chang, C.-H., Kettner, C. A. Kinetic and Crystallographic Studies of Thrombin with Ac-(D)Phe-Pro-boroArg-OH and Its Lysine, Amidine, Homolysine and Ornithine Analogs. Biochemistry 1995, 34, 3750-3757.
    • (1995) Biochemistry , vol.34 , pp. 3750-3757
    • Webber, P.C.1    Lee, S.-L.2    Lewandowski, F.A.3    Schadt, M.C.4    Chang, C.-H.5    Kettner, C.A.6
  • 16
    • 0023140814 scopus 로고
    • Crystallographic R-Factor Refinement by Molecular Dynamics
    • Brunger, A. T.; Kuriyan, J.; Karplus, M. Crystallographic R-Factor Refinement by Molecular Dynamics. Science 1987, 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 17
    • 0000082544 scopus 로고
    • CHAIN-a Crystallographic Modeling Program
    • Sack, J. S. CHAIN-a Crystallographic Modeling Program. J. Mol. Graphics 1988, 249, 224-225.
    • (1988) J. Mol. Graphics , vol.249 , pp. 224-225
    • Sack, J.S.1
  • 18
    • 0000538815 scopus 로고
    • Analytical Molecular Surface Calculation
    • Connolly, M. L. Analytical Molecular Surface Calculation. J. Appl. Crystallogr. 1983, 16, 548-558.
    • (1983) J. Appl. Crystallogr. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 19
    • 0021107965 scopus 로고
    • Solvent-Accessible Surfaces of Proteins and Nucleic Acids
    • Connolly, M. L. Solvent-Accessible Surfaces of Proteins and Nucleic Acids. Science 1983, 221, 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 21
  • 22
    • 14444285388 scopus 로고
    • X-Ray Study of the Molecular Structure of 4-Demethylhasubanonine p-Bromobenzenesulphonate
    • White, D. N. J.; McPhail, A. T.; Sim, G. A. X-Ray Study of the Molecular Structure of 4-Demethylhasubanonine p-Bromobenzenesulphonate. J. Chem. Soc., Perkin Trans. 2 1972, 1280- 1283.
    • (1972) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1280-1283
    • White, D.N.J.1    McPhail, A.T.2    Sim, G.A.3
  • 23
    • 0025188147 scopus 로고
    • Ab Initio Calculations on N-Methylmethanesulfonamide and Methyl Methanesulfonate for the Development of Force Field Torsional Parameters and Their Use in the Conform a tional Analysis of Some Novel Estrogens
    • Bindal, R. D.; Golab, J. T.; Katzenellenbogen, J. A. Ab Initio Calculations on N-Methylmethanesulfonamide and Methyl Methanesulfonate for the Development of Force Field Torsional Parameters and Their Use in the Conform a tional Analysis of Some Novel Estrogens. J. Am. Chem. Soc. 1990, 112, 7861-7868.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7861-7868
    • Bindal, R.D.1    Golab, J.T.2    Katzenellenbogen, J.A.3
  • 24
    • 14444284000 scopus 로고
    • Crystal structure of the cyclic tetramer from 3,5-dichloro-4-hydroxybenzenesulfonylchloride
    • Cevasco, G.; Penco, S.; Thea, S.; Busetti, V. J. Crystal structure of the cyclic tetramer from 3,5-dichloro-4-hydroxybenzenesulfonylchloride. Chem. Res. 1993, 102, 779-780.
    • (1993) Chem. Res. , vol.102 , pp. 779-780
    • Cevasco, G.1    Penco, S.2    Thea, S.3    Busetti, V.J.4
  • 26
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode, W.; Mayr, I.; Baumann, U.; Huber, R.; Stone, S. R.; Hofsteenge, J. The refined 1.9 Å crystal structure of human α-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989, 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
  • 30
    • 0022419375 scopus 로고
    • Aromatic-Aromatic Interaction: A Mechanism of Protein Structure Stabilization
    • Burley, S. K.; Petsko, G. A. Aromatic-Aromatic Interaction: A Mechanism of Protein Structure Stabilization. Science 1985, 229, 23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 33
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F. M. Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 1977, 6, 151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 34
    • 0000216832 scopus 로고    scopus 로고
    • The C-H⋯O Hydrogen Bond: Structural Implications and Supromolecular Design
    • Desiraju, G. The C-H⋯O Hydrogen Bond: Structural Implications and Supromolecular Design. Acc. Chem. Res. 1996, 29, 441-449.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 441-449
    • Desiraju, G.1
  • 35
    • 0001168372 scopus 로고
    • Intermolecular Interactions Around Functional Groups in Crystals: Data for Modeling the Binding of Drugs to Biological Macromolecules
    • Glusker, J. P. Intermolecular Interactions Around Functional Groups in Crystals: Data for Modeling the Binding of Drugs to Biological Macromolecules. Acta Crystallogr. 1995, D51, 418- 427.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 418-427
    • Glusker, J.P.1
  • 36
    • 33845554708 scopus 로고
    • Crystallographic Evidence for the Existence of C-H⋯O, C-H⋯N, and C-H⋯Cl Hydrogen Bonds
    • Taylor, R.; Kennard, O. Crystallographic Evidence for the Existence of C-H⋯O, C-H⋯N, and C-H⋯Cl Hydrogen Bonds. J. Am. Chem. Soc. 1982, 104, 5063-5070.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 5063-5070
    • Taylor, R.1    Kennard, O.2
  • 37
    • 0028978764 scopus 로고
    • The Occurrence of C-H⋯O Hydrogen Bonds in Proteins
    • Derewenda, Z. S.; Lee, L.; Derewenda, U. The Occurrence of C-H⋯O Hydrogen Bonds in Proteins. J. Mol. Biol. 1995, 252, 248-262.
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, U.3
  • 38
  • 39
    • 0006474999 scopus 로고
    • Role of C-H⋯O Hydrogen Bonds in the Coordination of Water Molecules. Analysis of Neutron Diffraction Data
    • Steiner, T.; Saenger, W. Role of C-H⋯O Hydrogen Bonds in the Coordination of Water Molecules. Analysis of Neutron Diffraction Data. J. Am. Chem. Soc. 1993, 115, 4540-4547.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4540-4547
    • Steiner, T.1    Saenger, W.2
  • 40
    • 0001515982 scopus 로고
    • 3 Bond in a Crystalline Hydrated Tricyclic Orthoamide: Evidence for C-H⋯O Hydrogen Bonds
    • 3 Bond in a Crystalline Hydrated Tricyclic Orthoamide: Evidence for C-H⋯O Hydrogen Bonds. Helv. Chim. Acta 1989, 72, 1125-1135.
    • (1989) Helv. Chim. Acta , vol.72 , pp. 1125-1135
    • Seiler, P.1    Dunitz, J.D.2
  • 41
    • 0002764112 scopus 로고
    • Water Molecules Which Apparently Accept No Hydrogen Bonds are Systematically Involved in C-H⋯O Interactions
    • Steiner, T. Water Molecules Which Apparently Accept No Hydrogen Bonds are Systematically Involved in C-H⋯O Interactions. Acta Crystallogr. 1995, D51, 93-97.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 93-97
    • Steiner, T.1
  • 42
    • 0001101390 scopus 로고
    • Small-Molecule Crystal Structures as a Structural Basis for Drug Design
    • Pascard, C. Small-Molecule Crystal Structures as a Structural Basis for Drug Design. Acta Crystallogr. 1995, D51, 407-417.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 407-417
    • Pascard, C.1
  • 43
    • 11744374008 scopus 로고
    • Dimerization Energetics of Benzene and Aromatic Amino Acid Side Chains
    • Burley, S. K.; Petsko, G. A. Dimerization Energetics of Benzene and Aromatic Amino Acid Side Chains. J. Am. Chem. Soc. 1986, 108, 7995-8001.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7995-8001
    • Burley, S.K.1    Petsko, G.A.2
  • 44
    • 0024260626 scopus 로고
    • Weakly Polar Interactions in Proteins
    • Burley, S. K.; Petsko, G. A. Weakly Polar Interactions in Proteins. Adv. Protein Chem. 1988, 39, 125-189.
    • (1988) Adv. Protein Chem. , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 45
    • 0021049880 scopus 로고
    • Waterlogged Molecules
    • Wolfenden, R. Waterlogged Molecules. Science 1983, 222, 1087- 1093.
    • (1983) Science , vol.222 , pp. 1087-1093
    • Wolfenden, R.1
  • 49
    • 0027435760 scopus 로고
    • Synthetic Selective Inhibitors of Thrombin
    • Okamoto, S.; Hijikata-Okunomiya, A. Synthetic Selective Inhibitors of Thrombin. Methods Enzymol. 1993, 222, 328-340.
    • (1993) Methods Enzymol. , vol.222 , pp. 328-340
    • Okamoto, S.1    Hijikata-Okunomiya, A.2


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