메뉴 건너뛰기




Volumn 43, Issue 3, 2000, Pages 361-368

Structural basis of the thrombin selectivity of a ligand that contains the constrained arginine mimic (2S)-2-amino-(3S)-3-(1-carbamimidoylpiperidin- 3-yl)-propanoic acid at P1

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 3 (1 CARBAMIMIDOYL PIPERIDIN 3 YL)PROPANOIC ACID; ARGININE DERIVATIVE; LIGAND; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 0034628521     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm990216f     Document Type: Article
Times cited : (16)

References (38)
  • 1
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie, E. W.; Fujikawa, K.; Kisiel, W. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991, 30, 10363-70.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 2
    • 0026102830 scopus 로고
    • Thrombin structure and function: Why thrombin is the primary target for antithrombotics
    • Fenton, J. W., II; Ofosu, F. A.; Moon, D. G.; Maraganore, J. M. Thrombin structure and function: why thrombin is the primary target for antithrombotics. Blood Coagulation Fibrinolysis 1991, 2, 69-75.
    • (1991) Blood Coagulation Fibrinolysis , vol.2 , pp. 69-75
    • Fenton J.W. II1    Ofosu, F.A.2    Moon, D.G.3    Maraganore, J.M.4
  • 3
    • 0027236253 scopus 로고
    • Thrombin, thrombin inhibitors, and the arterial thrombotic process
    • Maraganore, J. M. Thrombin, thrombin inhibitors, and the arterial thrombotic process. Thromb. Haemostasis 1993, 70, 208-11.
    • (1993) Thromb. Haemostasis , vol.70 , pp. 208-211
    • Maraganore, J.M.1
  • 4
    • 0000523854 scopus 로고
    • Hirudin and hirulog: Advances in antithrombotic therapy
    • Maraganore, J. M. Hirudin and hirulog: Advances in antithrombotic therapy. Perspect. Drug Discovery Des. 1994, 1, 461-78.
    • (1994) Perspect. Drug Discovery Des. , vol.1 , pp. 461-478
    • Maraganore, J.M.1
  • 15
    • 0027050807 scopus 로고
    • The refined 1.9-.ANG. X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human.alpha.-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode, W.; Turk, D.; Karshikov, A. The refined 1.9-.ANG. 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. 1992, 1, 426-71.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 16
    • 0025175641 scopus 로고
    • Geometry of binding of the benzamidine- and arginine-based inhibitors N.alpha.-(2-naphthyl-sulfonyl-glycyl)-DL-p-amidinophenylalanyl-piperidine (NAPAP) and (2R, 4R)-4-methyl-1-[N.alpha.-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulfonyl)-L- arginyl]-2-piperidine carboxylic acid (MQPA) to human.alpha.-thrombin
    • Bode, W.; Turk, D.; Stuerzebecher, J. Geometry of binding of the benzamidine- and arginine-based inhibitors N.alpha.-(2-naphthyl-sulfonyl-glycyl)-DL-p-amidinophenylalanyl-piperidine (NAPAP) and (2R, 4R)-4-methyl-1-[N.alpha.-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulfonyl)-L- arginyl]-2-piperidine carboxylic acid (MQPA) to human.alpha.-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin. Eur. J. Biochem. 1990, 193, 175-82.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 175-182
    • Bode, W.1    Turk, D.2    Stuerzebecher, J.3
  • 17
    • 0025851272 scopus 로고
    • Geometry of binding of the N.alpha.-tosylated piperidides of m-amidino-, p-amidino-and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes
    • Turk, D.; Stuerzebecher, J.; Bode, W. Geometry of binding of the N.alpha.-tosylated piperidides of m-amidino-, p-amidino-and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes. FEBS Lett. 1991, 287, 133-8.
    • (1991) Febs Lett. , vol.287 , pp. 133-138
    • Turk, D.1    Stuerzebecher, J.2    Bode, W.3
  • 22
    • 0032167901 scopus 로고    scopus 로고
    • Highly selective mechanism-based thrombin inhibitors: Structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes
    • Krishnan, R.; Zhang, E.; Hakansson, K.; Arni, R. K.; Tulinsky, A.; Lim-Wilby, M. S. L.; Levy, O. E.; Semple, J. E.; Brunck, T. K. Highly Selective Mechanism-Based Thrombin Inhibitors: Structures of Thrombin and Trypsin Inhibited with Rigid Peptidyl Aldehydes. Biochemistry 1998, 37, 12094-12103.
    • (1998) Biochemistry , vol.37 , pp. 12094-12103
    • Krishnan, R.1    Zhang, E.2    Hakansson, K.3    Arni, R.K.4    Tulinsky, A.5    Lim-Wilby, M.S.L.6    Levy, O.E.7    Semple, J.E.8    Brunck, T.K.9
  • 25
    • 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, 157-62.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 26
    • 0030977461 scopus 로고    scopus 로고
    • Therapeutic potential of trypsin-like serine protease inhibitors
    • Nakayama, Y.; Senokuchi, K.; Nakai, H.; Obata, T.; Kawamura, M. Therapeutic potential of trypsin-like serine protease inhibitors. Drugs Future 1997, 22, 285-293.
    • (1997) Drugs Future , vol.22 , pp. 285-293
    • Nakayama, Y.1    Senokuchi, K.2    Nakai, H.3    Obata, T.4    Kawamura, M.5
  • 28
    • 0022328790 scopus 로고
    • Calculation of molecular volumes and areas for structures of known geometry
    • Richards, F. M. Calculation of molecular volumes and areas for structures of known geometry. Methods Enzymol. 1985, 775, 440-64.
    • (1985) Methods Enzymol. , vol.775 , pp. 440-464
    • Richards, F.M.1
  • 29
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M. L. The molecular surface package. J. Mol. Graphics 1993, 11, 139-41.
    • (1993) J. Mol. Graphics , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 30
    • 0343572540 scopus 로고    scopus 로고
    • note
    • Note: Crystallographically obtained conformations of small molecules present as receptor complexes tend to have small variations in bond lengths, bond angles, and torsions from canonical values used by molecular mechanics force fields. This could translate to large strain energies when evaluated using molecular mechanics. Proper treatment of strain energies across four enzyme complexes where the inhibitors are covalently attached to the enzyme is beyond the scope of this work. Hence a comparison of strain energies for the bound conformations of the inhibitors is not considered.
  • 31
    • 0025923430 scopus 로고
    • Glu-192→Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin
    • Le Bonniec, B. F.; Esmon, C. T. Glu-192→Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 7371-5.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7371-7375
    • Le Bonniec, B.F.1    Esmon, C.T.2
  • 32
    • 0028174260 scopus 로고
    • Glu192→Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor
    • Guinto, E. R.; Ye, J.; Le Bonniec, B. F.; Esmon, C. T. Glu192→Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor. J. Biol. Chem. 1994, 269, 18395-400.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18395-18400
    • Guinto, E.R.1    Ye, J.2    Le Bonniec, B.F.3    Esmon, C.T.4
  • 33
    • 0029017446 scopus 로고
    • Alteration of the substrate and inhibitor specificities of blood coagulation factor VIIa: Importance of amino acid residue K192
    • Neuenschwander, P. F.; Morrissey, J. H. Alteration of the Substrate and Inhibitor Specificities of Blood Coagulation Factor VIIa: Importance of Amino Acid Residue K192. Biochemistry 1995, 34, 8701-7.
    • (1995) Biochemistry , vol.34 , pp. 8701-8707
    • Neuenschwander, P.F.1    Morrissey, J.H.2
  • 34
    • 0030847766 scopus 로고    scopus 로고
    • Protein data bank archives of three-dimensional macromolecular structures
    • Abola, E. E.; Sussman, J. L.; Prilusky, J.; Manning, N. O. Protein Data Bank archives of three-dimensional macromolecular structures. Methods Enzymol. 1997, 277, 556-571.
    • (1997) Methods Enzymol. , vol.277 , pp. 556-571
    • Abola, E.E.1    Sussman, J.L.2    Prilusky, J.3    Manning, N.O.4
  • 36
    • 0024791521 scopus 로고
    • Crystal structure of bovine.Beta.-trypsin at 1.5.ANG. Resolution in a crystal form with low molecular packing density. Active site geometry, ion pairs and solvent structure
    • Bartunik, H. D.; Summers, L. J.; Bartsch, H. H. Crystal structure of bovine.beta.-trypsin at 1.5.ANG. resolution in a crystal form with low molecular packing density. Active site geometry, ion pairs and solvent structure. J. Mol. Biol. 1989, 210, 813-28.
    • (1989) J. Mol. Biol. , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.