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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-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.

Original publication

DOI

10.1016/j.bbrc.2012.02.038

Type

Journal article

Journal

Biochemical and biophysical research communications

Publication Date

03/2012

Volume

419

Pages

485 - 489

Addresses

Structural Genomics Consortium, Oxford, UK.

Keywords

Humans, Zinc, Isoenzymes, Carbonic Anhydrases, Enzyme Inhibitors, Crystallography, X-Ray, Catalytic Domain, Protein Conformation, Protein Multimerization, Drug Discovery