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Publication Abstract from PubMed

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 1.9A crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. The active site cavity contains a cluster of non-conserved residues that may be involved in ligand binding and have significant implications for developing the next-generation of isoform-specific inhibitors.

Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.,Pilka ES, Kochan G, Oppermann U, Yue WW Biochem Biophys Res Commun. 2012 Mar 16;419(3):485-9. Epub 2012 Feb 14. PMID:22366092^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.