Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib

Bioorganic and Medicinal Chemistry Letters

Volumn 16, Issue 2, 2006, Pages 437-442

  Di Fiore, Anna ^a   Pedone, Carlo ^a,b   D'Ambrosio, Katia ^a   Scozzafava, Andrea ^c   De Simone, Giuseppina ^a   Supuran, Claudiu T ^c  

^a CNR   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Acetazolamide; Carbonic anhydrase; Celecoxib; COX 2 selective inhibitors; Isoform II; Sulfonamide; Valdecoxib; X ray crystallography

Indexed keywords

ACETAZOLAMIDE; ANALGESIC AGENT; AROMATIC COMPOUND; BENZENE DERIVATIVE; BENZENESULFONAMIDE DERIVATIVE; CARBONATE DEHYDRATASE INHIBITOR; CELECOXIB; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; DICLOFENAMIDE; DORZOLAMIDE; FUNCTIONAL GROUP; GLYCINE; ISOXAZOLE; ISOXAZOLE DERIVATIVE; LEUCINE; METHAZOLAMIDE; METHYL GROUP; PROLINE; THREONINE; VALDECOXIB; VALINE; ZINC ION;

ARTICLE; CHEMICAL BOND; CHEMICAL INTERACTION; CRYSTAL STRUCTURE; DRUG DESIGN; DRUG POTENCY; DRUG PROTEIN BINDING; ENZYME INHIBITION; GEOMETRY; HYDROPHOBICITY; SUBSTITUTION REACTION;

BINDING SITES; CARBONIC ANHYDRASE INHIBITORS; CARBONIC ANHYDRASES; CRYSTALLOGRAPHY, X-RAY; CYCLOOXYGENASE 2; CYCLOOXYGENASE INHIBITORS; DNA TOPOISOMERASES, TYPE II; DRUG EVALUATION, PRECLINICAL; HUMANS; ISOENZYMES; ISOXAZOLES; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PYRAZOLES; STRUCTURE-ACTIVITY RELATIONSHIP; SULFONAMIDES;

EID: 27944498514     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2005.09.040     Document Type: Article

References (30)

1. X. de Leval, F. Julémont, J. Delarge, V. Sanna, B. Pirotte, and J.-M. Dogné Expert Opin. Ther. Pat. 12 2002 969
2. C.T. Supuran, A. Casini, A. Mastrolorenzo, and A. Scozzafava Mini-Rev. Med. Chem. 4 2004 625
3. J.-M. Dogné, C.T. Supuran, and D. Pratico J. Med. Chem. 48 2005 2251
4. C.T. Supuran, A. Scozzafava, and A. Casini Med. Res. Rev. 23 2003 146
5. C.T. Supuran, and A. Scozzafava Expert Opin. Ther. Pat. 12 2002 217
6. A. Scozzafava, A. Mastrolorenzo, and C.T. Supuran Expert Opin. Ther. Pat. 14 2004 667
7. S. Pastorekova, S. Parkkila, J. Pastorek, and C.T. Supuran J. Enz. Inhib. Med. Chem. 19 2004 199
8. E. Švastová, A. Hulíková, M. Rafajová, M. Zatovicová, A. Gibadulinová, A. Casini, A. Cecchi, A. Scozzafava, C.T. Supuran, J. Pastorek, and S. Pastoreková FEBS Lett. 577 2004 439
9. A. Cecchi, A. Hulikova, J. Pastorek, S. Pastoreková, A. Scozzafava, J.-Y. Winum, J.-L. Montero, and C.T. Supuran J. Med. Chem. 48 2005 4834
10. A. Weber, A. Casini, A. Heine, D. Kuhn, C.T. Supuran, A. Scozzafava, and G. Klebe J. Med. Chem. 47 2004 550
11. D. Vullo, A. Innocenti, I. Nishimori, J. Pastorek, A. Scozzafava, S. Pastorekova, and C.T. Supuran Biorg. Med. Chem. Lett. 15 2005 963
12. Y. Pocker, and J.T. Stone Biochemistry 6 1967 668
13. 11
14. Supuran, C. T.; Scozzafava, A.; Conway, J., Eds.; Carbonic Anhydrase-Its Inhibitors and Activators; CRC Press: Boca Raton, FL, 2004; pp 1-363.
15. 17, were necessary to reduce the crystallographic R-factor and R-free values (in the 20.00-1.46 Å resolution range) to 0.185 and 0.200, respectively. The statistics for refinement are summarized in Table 2. Coordinates and structure factors have been deposited with the Protein Data Bank (Accession code 2AW1).
16. Z. Otwinowski, and W. Minor Methods Enzymol. 276 1997 307
17. A.T. Brünger, P.D. Adams, G.M. Clore, W.L. De Lano, P. Gros, R.W. Grosse-Kunstleve, J.S. Jiang, J. Kuszewski, M. Nilges, N.S. Pannu, R.J. Read, L.M. Rice, T. Simonson, and G.L. Warren Acta Crystallogr. Sect. D. 54 1998 905
18. T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Acta Crystallogr. Sect. A 47 1991 110
19. A.E. Eriksson, T.A. Jones, and A. Liljas Proteins Struct. Funct. 4 1988 274
20. F. Abbate, A. Casini, T. Owa, A. Scozzafava, and C.T. Supuran Bioorg. Med. Chem. Lett. 14 2004 217
21. F. Abbate, A. Casini, A. Scozzafava, and C.T. Supuran Bioorg. Med. Chem. Lett. 14 2004 2357
22. F. Abbate, A. Casini, A. Scozzafava, and C.T. Supuran J. Enzyme Inhib. Med. Chem. 18 2003 303
23. F. Abbate, A. Coetzee, A. Casini, S. Ciattini, A. Scozzafava, and C.T. Supuran Bioorg. Med. Chem. Lett. 14 2004 337
24. F. Abbate, C.T. Supuran, A. Scozzafava, P. Orioli, M. Stubbs, and G. Klebe J. Med. Chem. 45 2002 3583
25. F. Abbate, J.-Y. Winum, B.V.L. Potter, A. Casini, J.-L. Montero, A. Scozzafava, and C.T. Supuran Bioorg. Med. Chem. Lett. 14 2004 231
26. A. Casini, F. Abbate, A. Scozzafava, and C.T. Supuran Bioorg. Med. Chem. Lett. 13 2003 2763
27. A. Casini, J. Antel, F. Abbate, A. Scozzafava, S. David, H. Waldeck, S. Schä fer, and C.T. Supuran Bioorg. Med. Chem. Lett. 13 2003 841
28. A. Di Fiore, G. De Simone, V. Menchise, C. Pedone, A. Casini, A. Scozzafava, and C.T. Supuran Bioorg. Med. Chem. Lett. 15 2005 1937
29. G. De Simone, A. Di Fiore, V. Menchise, C. Pedone, J. Antel, A. Casini, A. Scozzafava, M. Wurl, and C.T. Supuran Bioorg. Med. Chem. Lett. 15 2005 2315
30. V. Menchise, G. De Simone, V. Alterio, A. Di Fiore, C. Pedone, A. Scozzafava, and C.T. Supuran J. Med. Chem. 48 2005 5721