메뉴 건너뛰기




Volumn 3, Issue 11, 1996, Pages 927-933

Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; NONSTEROID ANTIINFLAMMATORY AGENT; PROSTAGLANDIN SYNTHASE; PROSTAGLANDIN SYNTHASE INHIBITOR;

EID: 0029911267     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1196-927     Document Type: Article
Times cited : (569)

References (40)
  • 1
    • 0029086681 scopus 로고
    • Specificty of expression and effects of eicosanoid mediators in normal physiology and human diseases
    • Goetzl, E.J., An, S. & Smith, W.L. Specificty of expression and effects of eicosanoid mediators in normal physiology and human diseases. FASEB J. 9, 1051-1058 (1995).
    • (1995) FASEB J. , vol.9 , pp. 1051-1058
    • Goetzl, E.J.1    An, S.2    Smith, W.L.3
  • 2
    • 77956851758 scopus 로고
    • The eicosanoids: Cycloxygenase, lipoxygenase, and epoxygenase pathways
    • (eds. D.E. Vance and J. Vance) Elesvier Science Publishers
    • Smith, W.L., Borgeat P. & Fitzpatrick, F.A. The eicosanoids: cycloxygenase, lipoxygenase, and epoxygenase pathways, in Biochemistry of Lipids, Lipoproteins and Membranes (eds. D.E. Vance and J. Vance) 297-325 (Elesvier Science Publishers, 1991).
    • (1991) Biochemistry of Lipids, Lipoproteins and Membranes , pp. 297-325
    • Smith, W.L.1    Borgeat, P.2    Fitzpatrick, F.A.3
  • 3
    • 0025871150 scopus 로고
    • TIS10, a phorbol ester tumor promoter-inducible mRNA from swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase
    • Kujubu, D.A., Fletcher, B.S., Varnum, B.C., Lim, R.W. & Herschman, H.R. TIS10, a phorbol ester tumor promoter-inducible mRNA from swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase. J. Biol. Chem. 266, 12866-12872 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 12866-12872
    • Kujubu, D.A.1    Fletcher, B.S.2    Varnum, B.C.3    Lim, R.W.4    Herschman, H.R.5
  • 5
    • 0028047951 scopus 로고
    • Characterization of the genomic structure, chromosomal location and promoter of human prostaglandin H synthase-2 gene
    • Tazawa, R., Xu, X.M., Wu, K.K. & Wang, L.H. Characterization of the genomic structure, chromosomal location and promoter of human prostaglandin H synthase-2 gene. Biochem. Biophys. Res. Comm. 203, 190-199 (1994).
    • (1994) Biochem. Biophys. Res. Comm. , vol.203 , pp. 190-199
    • Tazawa, R.1    Xu, X.M.2    Wu, K.K.3    Wang, L.H.4
  • 6
    • 0028959950 scopus 로고
    • Regulation of Prostaglandin endoperoxide synthase (Cyclooxygenase) isozyme expression
    • Goppelt-Struebe, M. Regulation of Prostaglandin endoperoxide synthase (Cyclooxygenase) isozyme expression. Prostagl. Leukotr. Essen. Fatty Acids 52, 213-222 (1995).
    • (1995) Prostagl. Leukotr. Essen. Fatty Acids , vol.52 , pp. 213-222
    • Goppelt-Struebe, M.1
  • 7
    • 0028969527 scopus 로고
    • Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2
    • Morita, I. et al. Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2. J. Biol. Chem. 270, 10902-10908 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 10902-10908
    • Morita, I.1
  • 8
    • 0025888387 scopus 로고
    • Electron spin resonance investigation of tyrosyl radicals of prostaglandin H synthase: Relation to enzyme catalysis
    • Lassmann, G., Odenwaller, R., Curtis, J.F., DeGray, J.A., Mason, R.P., Marnett L.J. & Eling, T.E. Electron spin resonance investigation of tyrosyl radicals of prostaglandin H synthase: Relation to enzyme catalysis. J. Biol. Chem. 266, 20045-2055 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 20045-22055
    • Lassmann, G.1    Odenwaller, R.2    Curtis, J.F.3    DeGray, J.A.4    Mason, R.P.5    Marnett, L.J.6    Eling, T.E.7
  • 9
    • 0025202767 scopus 로고
    • Tyrosine 385 of prostaglandin endoperoxide synthase is required for cyclooxygenase catalysis
    • Shimokawa, T., Kulmacz, R.J., Dewitt, D.L. & Smith, W.L. Tyrosine 385 of prostaglandin endoperoxide synthase is required for cyclooxygenase catalysis. J. Biol. Chem. 265, 20073-20076 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 20073-20076
    • Shimokawa, T.1    Kulmacz, R.J.2    Dewitt, D.L.3    Smith, W.L.4
  • 10
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot, D., Loll, P.J. & Garavito, R.M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367, 243-249 (1994).
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 11
    • 0026508844 scopus 로고
    • Tyrosyl radicals and their role in hydroperoxide dependent activation and inactivation of prostaglandin endoperoxide synthase
    • Smith, W.L., Eling, T.E., Kulmacz, R.J., Marnett, L.J. & Tsai, A. Tyrosyl radicals and their role in hydroperoxide dependent activation and inactivation of prostaglandin endoperoxide synthase. Biochem. 31, 3-7 (1992).
    • (1992) Biochem. , vol.31 , pp. 3-7
    • Smith, W.L.1    Eling, T.E.2    Kulmacz, R.J.3    Marnett, L.J.4    Tsai, A.5
  • 12
    • 0028139275 scopus 로고
    • Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase
    • Copeland, R.A. et al. Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase. Proc. Natl. Acad. Sci. USA 91, 11202-11206 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11202-11206
    • Copeland, R.A.1
  • 13
    • 85143322198 scopus 로고
    • Crystallizing membrane proteins: Experiments on different systems
    • (eds. H. Michel) CRC Press, Boca Raton
    • Garavito, R.M. Crystallizing membrane proteins: Experiments on different systems, in Crystallization of Membrane Proteins (eds. H. Michel) 89-105 (CRC Press, Boca Raton, 1991).
    • (1991) Crystallization of Membrane Proteins , pp. 89-105
    • Garavito, R.M.1
  • 14
    • 0027992733 scopus 로고
    • Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system
    • Barnett J. et al. Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system. Bioch. Biophys. Acata 1209, 130-139 (1994).
    • (1994) Bioch. Biophys. Acata , vol.1209 , pp. 130-139
    • Barnett, J.1
  • 15
    • 0025366965 scopus 로고
    • Crystallography of biological macromolecules at ultra-low temperature
    • Hope, H. Crystallography of biological macromolecules at ultra-low temperature. Annu. Rev. Biophys. Biophys. Chem. 19, 107-126 (1990).
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 107-126
    • Hope, H.1
  • 17
    • 0028322893 scopus 로고
    • Selective inhibition of inducible cyclooxygenase 2 in vivo is antiinflammatory and nonulecerogenic
    • Masferrer, J.L. et al. Selective inhibition of inducible cyclooxygenase 2 in vivo is antiinflammatory and nonulecerogenic. Proc. Natl. Acad. Sci., USA 91, 3228-3232 (1994).
    • (1994) Proc. Natl. Acad. Sci., USA , vol.91 , pp. 3228-3232
    • Masferrer, J.L.1
  • 18
    • 0029204513 scopus 로고
    • The 3.1 Å X-ray crystal structure of the integral membrane enzyme prostaglandin H2 synthase-1
    • Garavito, R.M., Picot D. & Loll, P.J. The 3.1 Å X-ray crystal structure of the integral membrane enzyme prostaglandin H2 synthase-1. Adv. Prostagl. Throm. Leukotr. Res. 23, 99-103 (1995).
    • (1995) Adv. Prostagl. Throm. Leukotr. Res. , vol.23 , pp. 99-103
    • Garavito, R.M.1    Picot, D.2    Loll, P.J.3
  • 19
    • 0001099937 scopus 로고
    • Treatment of statistical errors in the determination of crystal structures
    • Luzzati, V. Treatment of statistical errors in the determination of crystal structures. Acta Crystallogr. 5, 802-810 (1952).
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 20
    • 0030010696 scopus 로고    scopus 로고
    • Synthesis and use of iodinated nonsteroidal antiinflammatory drug analogs as crystallographic probes of the the prostaglandin H2 cyclooxygenase active site
    • Loll, P.J., Picot, D., Ekabo, O. & Garavito, R.M. Synthesis and use of iodinated nonsteroidal antiinflammatory drug analogs as crystallographic probes of the the prostaglandin H2 cyclooxygenase active site. Biochem. 35, 7330-7340 (1996).
    • (1996) Biochem. , vol.35 , pp. 7330-7340
    • Loll, P.J.1    Picot, D.2    Ekabo, O.3    Garavito, R.M.4
  • 22
    • 0030063502 scopus 로고    scopus 로고
    • The kinetic factors that determine the affinity and selectivity for slow binding inhibition of human prostaglandin H synthase 1 and 2 by indomethicin and flurbiprofen
    • Callan, O.H., So, O. & Swinney, D. The kinetic factors that determine the affinity and selectivity for slow binding inhibition of human prostaglandin H synthase 1 and 2 by indomethicin and flurbiprofen. J. Biol. Chem. 271, 3548-3554 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 3548-3554
    • Callan, O.H.1    So, O.2    Swinney, D.3
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 24
    • 0029899186 scopus 로고    scopus 로고
    • A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors
    • Gierse, J.K. et al. A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors. J. Biol. Chem. 271, 15810-15814 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 15810-15814
    • Gierse, J.K.1
  • 25
    • 0029149067 scopus 로고
    • Fatty acid substrate specificites of human prostaglandin-enderoxide H synthase-1 and -2
    • Laneuville, O. et al. Fatty acid substrate specificites of human prostaglandin-enderoxide H synthase-1 and -2. J. Biol. Chem. 270, 19330-19336 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19330-19336
    • Laneuville, O.1
  • 26
    • 0015237292 scopus 로고
    • Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs
    • Vane, J.R. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nature New Biol. 231, 232-235 (1971).
    • (1971) Nature New Biol. , vol.231 , pp. 232-235
    • Vane, J.R.1
  • 27
    • 0025248570 scopus 로고
    • The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases
    • DeWitt, D.L. et al. The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases. J. Biol. Chem. 1990, 5192-5198 (1990).
    • (1990) J. Biol. Chem. , vol.1990 , pp. 5192-5198
    • DeWitt, D.L.1
  • 28
    • 0028339780 scopus 로고
    • Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin
    • Lecomte, M., Laneuville, O., Ji, C., DeWitt, D.L. & Smith, W.L. Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin. J. Biol. Chem. 269, 13207-13215 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 13207-13215
    • Lecomte, M.1    Laneuville, O.2    Ji, C.3    DeWitt, D.L.4    Smith, W.L.5
  • 29
    • 0028295135 scopus 로고
    • Mutation of serine-516 in human prostaglandin G/H synthase-2 to methionine and aspirin acetylation of this residue stimulates 15-R-HETE synthesis
    • Mancini, J.A., O'Neill, G.P., Bayly, C. & Vickers, P.J. Mutation of serine-516 in human prostaglandin G/H synthase-2 to methionine and aspirin acetylation of this residue stimulates 15-R-HETE synthesis. FEBS Lett. 342, 33-37 (1994).
    • (1994) FEBS Lett. , vol.342 , pp. 33-37
    • Mancini, J.A.1    O'Neill, G.P.2    Bayly, C.3    Vickers, P.J.4
  • 31
    • 0002452464 scopus 로고
    • Oscillation data reductions program
    • (eds. L. Sawyer, N. Isaacs and S. Bailey) SERC Daresbury Laboratory, UK
    • Otwinowski, Z. Oscillation data reductions program. in Proc. CCP4 Study Weekend, 29-30 Jan 1991. Data collection and processing (eds. L. Sawyer, N. Isaacs and S. Bailey) 55-62 SERC Daresbury Laboratory, UK, 1993).
    • (1993) Proc. CCP4 Study Weekend, 29-30 Jan 1991. Data Collection and Processing , pp. 55-62
    • Otwinowski, Z.1
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: Programs for protein crystallography. Acta Cryst. D50, 760-763 (1994).
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 34
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromoleuclar structures
    • Bernstein, F.C. et al. The protein data bank: A computer-based archival file for macromoleuclar structures. J. Mol. Biol. 112, 535-542 (1977).
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1
  • 35
    • 84944812221 scopus 로고
    • Extension of molecular replacment: A new search strategy based on Patterson correlation refinement
    • Brünger, A.T. Extension of molecular replacment: A new search strategy based on Patterson correlation refinement, Acta Crystallogr. A45, 46-57 (1990).
    • (1990) Acta Crystallogr. , vol.A45 , pp. 46-57
    • Brünger, A.T.1
  • 36
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474 (1992).
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 37
    • 0000349975 scopus 로고
    • MOLOC: A molecular modeling program
    • Muller, K. et al. MOLOC: A molecular modeling program. Bull. Soc. Chim. Belg. 97, 655-667 (1988).
    • (1988) Bull. Soc. Chim. Belg. , vol.97 , pp. 655-667
    • Muller, K.1
  • 38
    • 0026482961 scopus 로고
    • Tracking conformational states in allosteric transitions of phosphorylase
    • Browner, M.F., Fauman, E.B. & Fletterick, R.J. Tracking conformational states in allosteric transitions of phosphorylase. Biochemistry 31, 11297-11304 (1992).
    • (1992) Biochemistry , vol.31 , pp. 11297-11304
    • Browner, M.F.1    Fauman, E.B.2    Fletterick, R.J.3
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. App. Crystallgr. 24, 946-950 (1991).
    • (1991) J. App. Crystallgr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 40
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D.J. & Anderson, W.F. A fast algorithm for rendering space-filling molecule pictures. J. Molec. Graph. 6, 219-220 (1988).
    • (1988) J. Molec. Graph. , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.