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Volumn 412, Issue 2, 2011, Pages 235-250

The binding mechanism of a peptidic cyclic serine protease inhibitor

Author keywords

cancer; competitive inhibition; fibrinolysis

Indexed keywords

4 AMINOBENZAMIDINE; AMINO ACID; PLASMINOGEN ACTIVATOR INHIBITOR; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; UPAIN 1; UROKINASE;

EID: 80052022147     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.028     Document Type: Article
Times cited : (18)

References (40)
  • 2
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L. Serine protease mechanism and specificity Chem. Rev. 102 2002 4501 4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 3
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • Drag M., and Salvesen G.S. Emerging principles in protease-based drug discovery Nat. Rev. Drug. Discov. 9 2010 690 701
    • (2010) Nat. Rev. Drug. Discov. , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2
  • 4
    • 0036431989 scopus 로고    scopus 로고
    • Inhibitors of the protease domain of urokinase-type plasminogen activator
    • DOI 10.2174/1381612023392676
    • Rockway T.W., Nienaber V., and Giranda V.L. Inhibitors of the protease domain of urokinase-type plasminogen activator Curr. Pharm. Des. 8 2002 2541 2558 (Pubitemid 35331529)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.28 , pp. 2541-2558
    • Rockway, T.W.1    Nienaber, V.2    Giranda, V.L.3
  • 5
    • 0031610165 scopus 로고    scopus 로고
    • Selection of a cyclic nonapeptide inhibitor to α-chymotrypsin using a phage display peptide library
    • Krook M., Lindbladh C., Eriksen J.A., and Mosbach K. Selection of a cyclic nonapeptide inhibitor to α-chymotrypsin using a phage display peptide library Mol. Diversity 3 1997 149 159 (Pubitemid 127507548)
    • (1997) Molecular Diversity , vol.3 , Issue.3 , pp. 149-159
    • Krook, M.1    Lindbladh, C.2    Eriksen, J.A.3    Mosbach, K.4
  • 7
    • 0033776083 scopus 로고    scopus 로고
    • Identification of novel prostate-specific antigen-binding peptides modulating its enzyme activity
    • Wu P., Leinonen J., Koivunen E., Lankinen H., and Stenman U.H. Identification of novel prostate-specific antigen-binding peptides modulating its enzyme activity Eur. J. Biochem. 267 2000 6212 6220
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6212-6220
    • Wu, P.1    Leinonen, J.2    Koivunen, E.3    Lankinen, H.4    Stenman, U.H.5
  • 8
    • 67650305952 scopus 로고    scopus 로고
    • Phage-encoded combinatorial chemical libraries based on bicyclic peptides
    • Heinis C., Rutherford T., Freund S., and Winter G. Phage-encoded combinatorial chemical libraries based on bicyclic peptides Nat. Chem. Biol. 5 2009 502 507
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 502-507
    • Heinis, C.1    Rutherford, T.2    Freund, S.3    Winter, G.4
  • 10
    • 45349091918 scopus 로고    scopus 로고
    • A cyclic peptidylic inhibitor of murine urokinase-type plasminogen activator: Changing species specificity by substitution of a single residue
    • DOI 10.1042/BJ20071646
    • Andersen L.M., Wind T., Hansen H.D., and Andreasen P.A. A cyclic peptidylic inhibitor of murine urokinase-type plasminogen activator: changing species specificity by substitution of a single residue Biochem. J. 412 2008 447 457 (Pubitemid 351846410)
    • (2008) Biochemical Journal , vol.412 , Issue.3 , pp. 447-457
    • Andersen, L.M.1    Wind, T.2    Hansen, H.D.3    Andreasen, P.A.4
  • 12
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • DOI 10.1007/s000180050497
    • Andreasen P.A., Egelund R., and Petersen H.H. The plasminogen activation system in tumor growth, invasion, and metastasis Cell Mol. Life Sci. 57 2000 25 40 (Pubitemid 30105328)
    • (2000) Cellular and Molecular Life Sciences , vol.57 , Issue.1 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 14
    • 34548642972 scopus 로고    scopus 로고
    • Structural basis of specificity of a peptidyl urokinase inhibitor, upain-1
    • DOI 10.1016/j.jsb.2007.06.003, PII S1047847707001414
    • Zhao G., Yuan C., Wind T., Huang Z., Andreasen P.A., and Huang M. Structural basis of specificity of a peptidyl urokinase inhibitor, upain-1 J. Struct. Biol. 160 2007 1 10 (Pubitemid 47405230)
    • (2007) Journal of Structural Biology , vol.160 , Issue.1 , pp. 1-10
    • Zhao, G.1    Yuan, C.2    Wind, T.3    Huang, Z.4    Andreasen, P.A.5    Huang, M.6
  • 15
    • 0025883277 scopus 로고
    • Plasminogen activation by receptor-bound urokinase: A kinetic study with both cell-associated and isolated receptor
    • Ellis V., Behrendt N., and Dano K. Plasminogen activation by receptor-bound urokinase. A kinetic study with both cell-associated and isolated receptor J. Biol. Chem. 266 1991 12752 12758 (Pubitemid 21907159)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.19 , pp. 12752-12758
    • Ellis, V.1    Behrendt, N.2    Dano, K.3
  • 16
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz J.D. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions Chem. Biol. 2 1995 709 712
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 17
    • 0035107447 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Fact or artifact?
    • DOI 10.1110/ps.37801
    • Sharp K. Entropy-enthalpy compensation: fact or artifact? Protein Sci. 10 2001 661 667 (Pubitemid 32221155)
    • (2001) Protein Science , vol.10 , Issue.3 , pp. 661-667
    • Sharp, K.1
  • 18
    • 35748951604 scopus 로고    scopus 로고
    • Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition
    • DOI 10.1074/jbc.M704587200
    • Janssen B.J., Halff E.F., Lambris J.D., and Gros P. Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition J. Biol. Chem. 282 2007 29241 29247 (Pubitemid 350043342)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29241-29247
    • Janssen, B.J.C.1    Halff, E.F.2    Lambris, J.D.3    Gros, P.4
  • 19
    • 55649106334 scopus 로고    scopus 로고
    • Solution structure of the Grb2 SH2 domain complexed with a high-affinity inhibitor
    • Ogura K., Shiga T., Yokochi M., Yuzawa S., Burke T.R. Jr., and Inagaki F. Solution structure of the Grb2 SH2 domain complexed with a high-affinity inhibitor J. Biomol. NMR 42 2008 197 207
    • (2008) J. Biomol. NMR , vol.42 , pp. 197-207
    • Ogura, K.1    Shiga, T.2    Yokochi, M.3    Yuzawa, S.4    Burke, Jr.T.R.5    Inagaki, F.6
  • 20
    • 0036300518 scopus 로고    scopus 로고
    • Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor
    • DOI 10.1006/jmbi.2001.5370
    • Pan B., Li B., Russell S.J., Tom J.Y., Cochran A.G., and Fairbrother W.J. Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor J. Mol. Biol. 316 2002 769 787 (Pubitemid 34729253)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.3 , pp. 769-787
    • Pan, B.1    Li, B.2    Russell, S.J.3    Tom, J.Y.K.4    Cochran, A.G.5    Fairbrother, W.J.6
  • 21
    • 6344240541 scopus 로고    scopus 로고
    • Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes
    • Andrews M.J., McInnes C., Kontopidis G., Innes L., Cowan A., Plater A., and Fischer P.M. Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes Org. Biomol. Chem. 2 2004 2735 2741
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 2735-2741
    • Andrews, M.J.1    McInnes, C.2    Kontopidis, G.3    Innes, L.4    Cowan, A.5    Plater, A.6    Fischer, P.M.7
  • 24
    • 0036300793 scopus 로고    scopus 로고
    • Amino acid determinants of β-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library
    • DOI 10.1006/jmbi.2002.5410
    • Skelton N.J., Russell S., de Sauvage F., and Cochran A.G. Amino acid determinants of β-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library J. Mol. Biol. 316 2002 1111 1125 (Pubitemid 34729228)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.5 , pp. 1111-1125
    • Skelton, N.J.1    Russell, S.2    De Sauvage, F.3    Cochran, A.G.4
  • 26
    • 0029645121 scopus 로고
    • The crystal structure of the catalytic domain of human urokinase-type plasminogen activator
    • Spraggon G., Phillips C., Nowak U.K., Ponting C.P., Saunders D., and Dobson C.M. The crystal structure of the catalytic domain of human urokinase-type plasminogen activator Structure 3 1995 681 691
    • (1995) Structure , vol.3 , pp. 681-691
    • Spraggon, G.1    Phillips, C.2    Nowak, U.K.3    Ponting, C.P.4    Saunders, D.5    Dobson, C.M.6
  • 27
    • 0029587003 scopus 로고
    • Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes
    • Olson S.T., Bock P.E., Kvassman J., Shore J.D., Lawrence D.A., Ginsburg D., and Bjork I. Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes J. Biol. Chem. 270 1995 30007 30017
    • (1995) J. Biol. Chem. , vol.270 , pp. 30007-30017
    • Olson, S.T.1    Bock, P.E.2    Kvassman, J.3    Shore, J.D.4    Lawrence, D.A.5    Ginsburg, D.6    Bjork, I.7
  • 28
    • 0034832988 scopus 로고    scopus 로고
    • Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: Relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme
    • DOI 10.1046/j.1432-1327.2001.02365.x
    • Petersen H.H., Hansen M., Schousboe S.L., and Andreasen P.A. Localisation of epitopes for monoclonal anti-urokinase-type plasminogen activator antibodies. Relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme Eur. J. Biochem. 268 2001 4430 4439 (Pubitemid 32862852)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.16 , pp. 4430-4439
    • Petersen, H.H.1    Hansen, M.2    Schousboe, S.L.3    Andreasen, P.A.4
  • 29
    • 0016850356 scopus 로고
    • Characterization of the ultraviolet absorption spectra of para-substituted derivatives of benzamidine
    • Rogana E., Nelson D.L., and Mares-Guia M. Characterization of the ultraviolet absorption spectra of para-substituted derivatives of benzamidine J. Am. Chem. Soc. 97 1975 6844 6848
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 6844-6848
    • Rogana, E.1    Nelson, D.L.2    Mares-Guia, M.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Ccp4
    • CCP4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 34
    • 0031888668 scopus 로고    scopus 로고
    • Solution structure of Compstatin, a potent complement inhibitor
    • Morikis D., Assa-Munt N., Sahu A., and Lambris J.D. Solution structure of Compstatin, a potent complement inhibitor Protein Sci. 7 1998 619 627 (Pubitemid 28130884)
    • (1998) Protein Science , vol.7 , Issue.3 , pp. 619-627
    • Morikis, D.1    Assa-Munt, N.2    Sahu, A.3    Lambris, J.D.4
  • 35
    • 0034711003 scopus 로고    scopus 로고
    • Structures of the contryphan family of cyclic peptides. Role of electrostatic interactions in cis-trans isomerism
    • Pallaghy P.K., He W., Jimenez E.C., Olivera B.M., and Norton R.S. Structures of the contryphan family of cyclic peptides. Role of electrostatic interactions in cis-trans isomerism Biochemistry 39 2000 12845 12852
    • (2000) Biochemistry , vol.39 , pp. 12845-12852
    • Pallaghy, P.K.1    He, W.2    Jimenez, E.C.3    Olivera, B.M.4    Norton, R.S.5
  • 36
    • 0004040543 scopus 로고    scopus 로고
    • University of California San Francisco
    • Goddard T.D., and Kneller D.G. SPARKY 3 2002 University of California San Francisco
    • (2002) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 39
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • Nilges M., Gronenborn A.M., Brunger A.T., and Clore G.M. Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2 Protein Eng. 2 1988 27 38
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brunger, A.T.3    Clore, G.M.4
  • 40
    • 0030621858 scopus 로고    scopus 로고
    • Torsion-Angle Molecular Dynamics as a New Efficient Tool for NMR Structure Calculation
    • Stein E.G., Rice L.M., and Brunger A.T. Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation J. Magn. Reson. 124 1997 154 164 (Pubitemid 127451396)
    • (1997) Journal of Magnetic Resonance , vol.124 , Issue.1 , pp. 154-164
    • Stein, E.G.1    Rice, L.M.2    Brunger, A.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.