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Publication Abstract from PubMed

Human carbonic anhydrase VII (hCA VII) is a cytosolic member of the alpha-CA family. This enzyme is mainly localized in a number of brain tissues such as the cortex, hippocampus and thalamus and has been noted for its contribution in generating neuronal excitation and seizures. Recently, it has been also proposed that hCA VII may be involved in the control of neuropathic pain, thus its inhibition may offer a new approach in designing pain killers useful for combating neuropathic pain. We report here the X-ray crystallographic structure of a mutated form of human CA VII in complex with acetazolamide, a classical sulfonamide inhibitor. These crystallographic studies provide important implications for the rational drug design of selective CA inhibitors with clinical applications.

Crystal structure of the C183S/C217S mutant of human CA VII in complex with acetazolamide.,Di Fiore A, Truppo E, Supuran CT, Alterio V, Dathan N, Bootorabi F, Parkkila S, Monti SM, De Simone G Bioorg Med Chem Lett. 2010 Sep 1;20(17):5023-6. Epub 2010 Jul 16. PMID:20688517^[1]

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