Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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

Biochem Biophys Res Commun

Publication Date

16/03/2012

Volume

419

Pages

485 - 489

Keywords

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