Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 65, Issue -, Pages 992-995Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109036665
Keywords
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Funding
- National Institutes of Health [GM25154]
- Maren Foundation
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The crystal structure of human carbonic anhydrase II ( CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 angstrom resolution and refined to an R-cryst of 11.2% and an R-free of 14.7%. As observed in previous CA II-inhibitor complexes, AZM binds directly to the zinc and makes several key interactions with active-site residues. The high-resolution data also showed a glycerol molecule adjacent to the AZM in the active site and two additional AZMs that are adventitiously bound on the surface of the enzyme. The cobinding of AZM and glycerol in the active site demonstrate that given an appropriate ring orientation and substituents, an isozyme-specific CA inhibitor may be developed.
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