Journal
BIOMED RESEARCH INTERNATIONAL
Volume 2014, Issue -, Pages -Publisher
HINDAWI LTD
DOI: 10.1155/2014/389869
Keywords
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Funding
- Technology Agency of the Czech Republic [TE01020028]
- Academy of Sciences of the Czech Republic [RVO 68378050, 61388963]
- Czech Science Foundation [P208/12/G016]
- operational program Research and Development for Innovations of the European Social Fund [CZ1.05/2.1.00/03/0058]
- Gilead Sciences
- IOCB Research Centre
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Carborane-based compounds are promising lead structures for development of inhibitors of carbonic anhydrases (CAs). Here, we report structural and computational analysis applicable to structure-based design of carborane compounds with selectivity toward the cancer-specific CAIX isoenzyme. We determined the crystal structure of CAII in complex with 1-methylenesulfamide-1,2-dicarba-closo-dodecaborane at 1.0 angstrom resolution and used this structure to model the 1-methylenesulfamide-1,2-dicarba-closododecaborane interactions with CAIX. A virtual glycine scan revealed the contributions of individual residues to the energy of binding of 1-methylenesulfamide-1,2-dicarba-closo-dodecaborane to CAII and CAIX, respectively.
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