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American Chemical Society, Journal of Medicinal Chemistry, 7(54), p. 2522-2526, 2011

DOI: 10.1021/jm2000213

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Structural Basis for the Interaction Between Carbonic Anhydrase and 1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamides.

Journal article published in 2011 by Pavel Mader ORCID, Jiří Brynda, Rosaria Gitto, Stefano Agnello, Petr Pachl, Pavlína Řezáčová, Claudiu T. Supuran, Alba Chimirri, P. Rezachova, Pavlína Řezáčová
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Isoquinolinesulfonamides inhibit human carbonic anhydrases (hCAs) and display selectivity toward therapeutically relevant isozymes. The crystal structure of hCA II in complex with 6,7-dimethoxy-1-methyl-1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamide revealed unusual inhibitor binding. Structural analyses allowed for discerning the fine details of the inhibitor binding mode to the active site, thus providing clues for the future design of even more selective inhibitors for druggable isoforms such as the cancer associated hCA IX and neuronal hCA VII.