Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide

Anna Di Fiore, Simona Maria Monti, Mika Hilvo, Seppo Parkkila, Vincenza Romano, Andrea Scaloni, Carlo Pedone, Andrea Scozzafava, Claudiu T. Supuran, Giuseppina De Simone (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

90 Citations (Scopus)


The cytosolic isoform XIII is a recently discovered member of the human carbonic anhydrase (hCA, EC family. It is selectively expressed among other tissues in the reproductive organs, where it may control pH and ion balance regulation, ensuring thus proper fertilization conditions. The authors report here the X-ray crystallographic structure of this isozyme in the unbound state and in complex with a classical sulfonamide inhibitor, namely acetazolamide. A detailed comparison of the obtained structural data with those already reported for other CA isozymes provides novel insights into the catalytic properties of the members of this protein family. On the basis of the inhibitory properties of acetazolamide against various cytosolic/transmembrane isoforms and the structural differences detected within the active site of the various CA isoforms, further prospects for the design of isozyme-specific CA inhibitors are here proposed. Proteins 2009.
Original languageEnglish
Pages (from-to)164-175
Issue number1
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed


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