Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.

Journal article

Zn(2+)-dependent carbonic anhydrases (CA) catalyse the reversible hydration of carbon dioxide to bicarbonate and participate in diverse physiological processes, hence having manifold therapeutic potentials. Among the 15 human CAs with wide-ranging sub-cellular localisation and kinetic properties, CA VI is the only secretory isoform. The 1.9Å crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously...

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Authors: Pilka, E; Kochan, G; Oppermann, U; Yue, W

• Publication status: Published
• Journal: Biochemical and biophysical research communications
• Volume: 419
• Issue: 3
• Pages: 485-489
• Publication date: 2012-03-01
• DOI: 10.1016/j.bbrc.2012.02.038
• EISSN: 1090-2104
• ISSN: 0006-291X
• Language: English
• Keywords: Enzyme Inhibitors; Humans; Zinc; Crystallography, X-Ray; Catalytic Domain; Isoenzymes; Protein Conformation; Protein Multimerization; Drug Discovery; Carbonic Anhydrases