Positions of His‐64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors
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J J Baldwin | J. Springer | G. M. Smith | D. Christianson | B. McKeever | R. Alexander | G. Ponticello | W. Randall | J. Baldwin | C. N. Habecker | R S Alexander | D W Christianson | W C Randall | J P Springer | G M Smith | B M McKeever | G S Ponticello | C N Habecker
[1] D. Rich,et al. Pepstatin-derived inhibitors of aspartic proteinases. A close look at an apparent transition-state analogue inhibitor. , 1985, Journal of medicinal chemistry.
[2] M. James,et al. Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[3] D. Silverman,et al. Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant. , 1989, Biochemistry.
[4] V. Luzzati,et al. Traitement statistique des erreurs dans la determination des structures cristallines , 1952 .
[5] C. Fierke,et al. Conformational mobility of His-64 in the Thr-200----Ser mutant of human carbonic anhydrase II. , 1991, Biochemistry.
[6] W. Hendrickson. Stereochemically restrained refinement of macromolecular structures. , 1985, Methods in enzymology.
[7] S. Nair,et al. Unexpected Ph-Dependent Conformation of His-64, the Proton Shuttle of Carbonic Anhydrase II. , 1992 .
[8] T A Jones,et al. Refined structure of human carbonic anhydrase II at 2.0 Å resolution , 1988, Proteins.
[9] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[10] J J Baldwin,et al. Thienothiopyran-2-sulfonamides: novel topically active carbonic anhydrase inhibitors for the treatment of glaucoma. , 1989, Journal of medicinal chemistry.
[11] T. Maren,et al. Carbonic anhydrase: chemistry, physiology, and inhibition. , 1967, Physiological reviews.
[12] A T Brünger,et al. Slow-cooling protocols for crystallographic refinement by simulated annealing. , 1990, Acta crystallographica. Section A, Foundations of crystallography.
[13] W. Osborne,et al. An improved method for the purification of carbonic anhydrase isozymes by affinity chromatography. , 1975, Analytical biochemistry.
[14] M. James,et al. Structure and refinement of penicillopepsin at 1.8 A resolution. , 1983, Journal of molecular biology.
[15] A. Wilson,et al. Determination of Absolute from Relative X-Ray Intensity Data , 1942, Nature.
[16] L Järup,et al. Crystal structure of human carbonic anhydrase C. , 1972, Nature: New biology.
[17] D. Davies,et al. Three-dimensional structure of the complex of the Rhizopus chinensis carboxyl proteinase and pepstatin at 2.5-A resolution. , 1982, Biochemistry.
[18] M. Murcko,et al. New isomeric classes of topically active ocular hypotensive carbonic anhydrase inhibitors: 5-substituted thieno[2,3-b]thiophene-2-sulfonamides and 5-substituted thieno[3,2-b]thiophene-2-sulfonamides. , 1991, Journal of medicinal chemistry.
[19] Olga Kennard,et al. Systematic analysis of structural data as a research technique in organic chemistry , 1983 .
[20] J. Sack,et al. CHAIN — A crystallographic modeling program , 1988 .
[21] R J Lynch,et al. Design and synthesis of P2-P1'-linked macrocyclic human renin inhibitors. , 1991, Journal of medicinal chemistry.
[22] Y. Pocker,et al. Carbonic anhydrase: structure catalytic versatility, and inhibition. , 1978, Advances in enzymology and related areas of molecular biology.
[23] U. R. Evans,et al. Distribution of Attack on Iron or Zinc Partly Immersed in Chloride Solutions , 1942, Nature.
[24] W. Jencks,et al. Binding energy, specificity, and enzymic catalysis: the circe effect. , 2006, Advances in enzymology and related areas of molecular biology.