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Volumn 289, Issue 10, 2014, Pages 6799-6808

Oxicams bind in a novel mode to the cyclooxygenase active site via a two-water-mediated h-bonding network

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84896765443     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.517987     Document Type: Article
Times cited : (95)

References (41)
  • 1
    • 0036669556 scopus 로고    scopus 로고
    • Recent developments in cyclooxygenase inhibition
    • Marnett, L. J. (2002) Recent developments in cyclooxygenase inhibition. Prostaglandins Other Lipid Mediat. 68, 153-164
    • (2002) Prostaglandins Other Lipid Mediat. , vol.68 , pp. 153-164
    • Marnett, L.J.1
  • 3
    • 78049405035 scopus 로고    scopus 로고
    • Molecular basis for cyclooxygenase inhibition by the non-steroidal anti-inflammatory drug naproxen
    • Duggan, K. C., Walters, M. J., Musee, J., Harp, J. M., Kiefer, J. R., Oates, J. A., and Marnett, L. J. (2010) Molecular basis for cyclooxygenase inhibition by the non-steroidal anti-inflammatory drug naproxen. J. Biol. Chem. 285, 34950-34959
    • (2010) J. Biol. Chem. , vol.285 , pp. 34950-34959
    • Duggan, K.C.1    Walters, M.J.2    Musee, J.3    Harp, J.M.4    Kiefer, J.R.5    Oates, J.A.6    Marnett, L.J.7
  • 5
    • 34948902032 scopus 로고    scopus 로고
    • Structural basis of enantioselective inhibition of cyclooxygenase-1 by S-substituted indomethacin ethanolamides
    • Harman, C. A., Turman, M. V., Kozak, K. R., Marnett, L. J., Smith, W. L., and Garavito, R. M. (2007) Structural basis of enantioselective inhibition of cyclooxygenase-1 by S-substituted indomethacin ethanolamides. J. Biol. Chem. 282, 28096-28105
    • (2007) J. Biol. Chem. , vol.282 , pp. 28096-28105
    • Harman, C.A.1    Turman, M.V.2    Kozak, K.R.3    Marnett, L.J.4    Smith, W.L.5    Garavito, R.M.6
  • 8
    • 0035339905 scopus 로고    scopus 로고
    • Structural analysis of NSAID binding by prostaglandin H2 synthase: Time-dependent and time-independent inhibitors elicit identical enzyme conformations
    • Selinsky, B. S., Gupta, K., Sharkey, C. T., and Loll, P. J. (2001) Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Biochemistry 40, 5172-5180
    • (2001) Biochemistry , vol.40 , pp. 5172-5180
    • Selinsky, B.S.1    Gupta, K.2    Sharkey, C.T.3    Loll, P.J.4
  • 9
    • 0028009093 scopus 로고
    • The x-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot, D., Loll, P. J., and Garavito, R. M. (1994) The x-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367, 243-249
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 10
    • 0029056992 scopus 로고
    • The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase
    • Loll, P. J., Picot, D., and Garavito, R. M. (1995) The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase. Nat. Struct. Biol. 2, 637-643
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 637-643
    • Loll, P.J.1    Picot, D.2    Garavito, R.M.3
  • 12
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2
    • Luong, C., Miller, A., Barnett, J., Chow, J., Ramesha, C., and Browner, M. F. (1996) Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2. Nat. Struct. Biol. 3, 927-933
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 927-933
    • Luong, C.1    Miller, A.2    Barnett, J.3    Chow, J.4    Ramesha, C.5    Browner, M.F.6
  • 13
    • 68249100483 scopus 로고    scopus 로고
    • Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid
    • Prusakiewicz, J. J., Duggan, K. C., Rouzer, C. A., and Marnett, L. J. (2009) Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid. Biochemistry 48, 7353-7355
    • (2009) Biochemistry , vol.48 , pp. 7353-7355
    • Prusakiewicz, J.J.1    Duggan, K.C.2    Rouzer, C.A.3    Marnett, L.J.4
  • 14
    • 0034665857 scopus 로고    scopus 로고
    • The productive conformation of arachidonic acid bound to prostaglandin synthase
    • Malkowski, M. G., Ginell, S. L., Smith, W. L., and Garavito, R. M. (2000) The productive conformation of arachidonic acid bound to prostaglandin synthase. Science 289, 1933-1937
    • (2000) Science , vol.289 , pp. 1933-1937
    • Malkowski, M.G.1    Ginell, S.L.2    Smith, W.L.3    Garavito, R.M.4
  • 15
    • 77954611060 scopus 로고    scopus 로고
    • Structural basis of fatty acid substrate binding to cyclooxygenase-2
    • Vecchio, A. J., Simmons, D. M., and Malkowski, M. G. (2010) Structural basis of fatty acid substrate binding to cyclooxygenase-2. J. Biol. Chem. 285, 22152-22163
    • (2010) J. Biol. Chem. , vol.285 , pp. 22152-22163
    • Vecchio, A.J.1    Simmons, D.M.2    Malkowski, M.G.3
  • 17
    • 0032994274 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of meloxicam: A cyclo-oxygenase-2 preferential nonsteroidal anti-inflammatory drug
    • Davies, N. M., and Skjodt, N. M. (1999) Clinical pharmacokinetics of meloxicam: a cyclo-oxygenase-2 preferential nonsteroidal anti-inflammatory drug. Clin. Pharmacokinet. 36, 115-126
    • (1999) Clin. Pharmacokinet. , vol.36 , pp. 115-126
    • Davies, N.M.1    Skjodt, N.M.2
  • 18
    • 0029878866 scopus 로고    scopus 로고
    • Meloxicam
    • discussion 431-432
    • Noble, S., and Balfour, J. A. (1996) Meloxicam. Drugs 51, 424-430; discussion 431-432
    • (1996) Drugs , vol.51 , pp. 424-430
    • Noble, S.1    Balfour, J.A.2
  • 22
    • 78149333927 scopus 로고    scopus 로고
    • First-principles prediction of the pKas of anti-inflammatory oxicams
    • Ho, J., Coote, M. L., Franco-Pérez, M., and Gómez-Balderas, R. (2010) First-principles prediction of the pKas of anti-inflammatory oxicams. J. Phys. Chem. A 114, 11992-12003
    • (2010) J. Phys. Chem. A , vol.114 , pp. 11992-12003
    • Ho, J.1    Coote, M.L.2    Franco-Pérez, M.3    Gómez-Balderas, R.4
  • 23
    • 20344396413 scopus 로고    scopus 로고
    • Free energy perturbation approach to the critical assessment of selective cyclooxygenase-2 inhibitors
    • Park, H., and Lee, S. (2005) Free energy perturbation approach to the critical assessment of selective cyclooxygenase-2 inhibitors. J. Comput. Aided Mol. Des. 19, 17-31
    • (2005) J. Comput. Aided Mol. Des. , vol.19 , pp. 17-31
    • Park, H.1    Lee, S.2
  • 24
    • 0035258240 scopus 로고    scopus 로고
    • Recognition of cyclooxygenase-2 (COX-2) active site by NSAIDs: A computer modelling study
    • Kothekar, V., Sahi, S., Srinivasan, M., Mohan, A., and Mishra, J. (2001) Recognition of cyclooxygenase-2 (COX-2) active site by NSAIDs: a computer modelling study. Indian J. Biochem. Biophys. 38, 56-63
    • (2001) Indian J. Biochem. Biophys. , vol.38 , pp. 56-63
    • Kothekar, V.1    Sahi, S.2    Srinivasan, M.3    Mohan, A.4    Mishra, J.5
  • 25
    • 0025182574 scopus 로고
    • Preparation and proteolytic cleavage of apoprostaglandin endoperoxide synthase
    • Odenwaller, R., Chen, Y. N., and Marnett, L. J. (1990) Preparation and proteolytic cleavage of apoprostaglandin endoperoxide synthase. Methods Enzymol. 187, 479-485
    • (1990) Methods Enzymol. , vol.187 , pp. 479-485
    • Odenwaller, R.1    Chen, Y.N.2    Marnett, L.J.3
  • 26
    • 0032548140 scopus 로고    scopus 로고
    • Covalent modification of cyclooxygenase-2 (COX-2) by 2-acetoxyphenyl alkyl sulfides, a new class of selective COX-2 inactivators
    • Kalgutkar, A. S., Kozak, K. R., Crews, B. C., Hochgesang, G. P., Jr., and Marnett, L. J. (1998) Covalent modification of cyclooxygenase-2 (COX-2) by 2-acetoxyphenyl alkyl sulfides, a new class of selective COX-2 inactivators. J. Med. Chem. 41, 4800-4818
    • (1998) J. Med. Chem. , vol.41 , pp. 4800-4818
    • Kalgutkar, A.S.1    Kozak, K.R.2    Crews, B.C.3    Hochgesang Jr., G.P.4    Marnett, L.J.5
  • 27
    • 79956290893 scopus 로고    scopus 로고
    • Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer
    • Dong, L., Vecchio, A. J., Sharma, N. P., Jurban, B. J., Malkowski, M. G., and Smith, W. L. (2011) Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer. J. Biol. Chem. 286, 19035-19046
    • (2011) J. Biol. Chem. , vol.286 , pp. 19035-19046
    • Dong, L.1    Vecchio, A.J.2    Sharma, N.P.3    Jurban, B.J.4    Malkowski, M.G.5    Smith, W.L.6
  • 29
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32-41
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 32
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf, A. W., and van Aalten, D. M. (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    Van Aalten, D.M.2
  • 33
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 35
    • 0345735668 scopus 로고    scopus 로고
    • The 2. 0 A resolution crystal structure of prostaglandin H-2 synthase-1: Structural insights into an unusual peroxidase
    • Gupta, K., Selinsky, B. S., Kaub, C. J., Katz, A. K., and Loll, P. J. (2004) The 2.0 A resolution crystal structure of prostaglandin H-2 synthase-1: structural insights into an unusual peroxidase. J. Mol. Biol. 335, 503-518
    • (2004) J. Mol. Biol. , vol.335 , pp. 503-518
    • Gupta, K.1    Selinsky, B.S.2    Kaub, C.J.3    Katz, A.K.4    Loll, P.J.5
  • 36
    • 79958009684 scopus 로고    scopus 로고
    • The structural basis of endocannabinoid oxygenation by cyclooxygenase-2
    • Vecchio, A. J., and Malkowski, M. G. (2011) The structural basis of endocannabinoid oxygenation by cyclooxygenase-2. J. Biol. Chem. 286, 20736-20745
    • (2011) J. Biol. Chem. , vol.286 , pp. 20736-20745
    • Vecchio, A.J.1    Malkowski, M.G.2
  • 37
    • 84863794061 scopus 로고    scopus 로고
    • Investigating substrate promiscuity in cyclooxygenase-2: The role of Arg-120 and residues lining the hydrophobic groove
    • Vecchio, A. J., Orlando, B. J., Nandagiri, R., and Malkowski, M. G. (2012) Investigating substrate promiscuity in cyclooxygenase-2: the role of Arg-120 and residues lining the hydrophobic groove. J. Biol. Chem. 287, 24619-24630
    • (2012) J. Biol. Chem. , vol.287 , pp. 24619-24630
    • Vecchio, A.J.1    Orlando, B.J.2    Nandagiri, R.3    Malkowski, M.G.4
  • 38
    • 84856397848 scopus 로고    scopus 로고
    • A force field with discrete displaceable waters and desolvation entropy for hydrated ligand docking
    • Forli, S., and Olson, A. J. (2012) A force field with discrete displaceable waters and desolvation entropy for hydrated ligand docking. J. Med. Chem. 55, 623-638
    • (2012) J. Med. Chem. , vol.55 , pp. 623-638
    • Forli, S.1    Olson, A.J.2
  • 39
    • 0015184521 scopus 로고
    • Synthesis and antiinflammatory activity of some 3-carboxamides of 2-alkyl-4-hydroxy-2H-1,2-benzothiazine 1,1-dioxide
    • Lombardino, J. G., Wiseman, E. H., and McLamore, W. M. (1971) Synthesis and antiinflammatory activity of some 3-carboxamides of 2-alkyl-4-hydroxy-2H-1, 2-benzothiazine 1,1-dioxide. J. Med. Chem. 14, 1171-1175
    • (1971) J. Med. Chem. , vol.14 , pp. 1171-1175
    • Lombardino, J.G.1    Wiseman, E.H.2    McLamore, W.M.3
  • 40
    • 0023244957 scopus 로고
    • Analogues and derivatives of tenoxicam. Synthesis and antiinflammatory activity of analogues with different residues on the ring nitrogen and the amide nitrogen
    • Binder, D., Hromatka, O., Geissler, F., Schmied, K., Noe, C. R., Burri, K., Pfister, R., Strub, K., and Zeller, P. (1987) Analogues and derivatives of tenoxicam. Synthesis and antiinflammatory activity of analogues with different residues on the ring nitrogen and the amide nitrogen. J. Med. Chem. 30, 678-682
    • (1987) J. Med. Chem. , vol.30 , pp. 678-682
    • Binder, D.1    Hromatka, O.2    Geissler, F.3    Schmied, K.4    Noe, C.R.5    Burri, K.6    Pfister, R.7    Strub, K.8    Zeller, P.9


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