X-ray Crystallographic Studies Reveal That the Incorporation of Spacer Groups in Carbonic Anhydrase Inhibitors Causes Alternate Binding Modes.
From: Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Acta crystallographica. Section F, Structural biology and crystallization communications
- Publish Date: Jul 2006
- ISSN: 1744-3091
- Volume: 62
- Issue: Pt 7
- Pages: 618-22
- Medium: Internet
- Language: English
- Citation (JAMA): Fisher S Zoë, Govindasamy Lakshmanan, Boyle Nicholas, et al. X-ray Crystallographic Studies Reveal That the Incorporation of Spacer Groups in Carbonic Anhydrase Inhibitors Causes Alternate Binding Modes.. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Jul 2006;62:618-22
Abstract
Human carbonic anhydrases (CAs) are well studied targets for the development of inhibitors for pharmaceutical applications. The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a -CF2- or -CHNH2- spacer group. The structures presented here reveal that these spacer groups allow novel binding modes for the thiadiazole moiety compared with conventional CAIs.
Mesh Headings (Keywords): Binding Sites, Carbonic Anhydrases, Enzyme Inhibitors, Kinetics, Models, Molecular
Check for Full Text / PubMed Unique Identifier (PMID): 16820676
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