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Carborane-based carbonic anhydrase inhibitors: insight into CAII/CAIX specificity from a high-resolution crystal structure, modeling, and quantum chemical calculations

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    0440100 - ÚMG 2015 RIV US eng J - Journal Article
    Mader, Pavel - Pecina, Adam - Cígler, Petr - Lepšík, Martin - Šícha, Václav - Hobza, Pavel - Grüner, Bohumír - Fanfrlík, Jindřich - Brynda, Jiří - Řezáčová, Pavlína
    Carborane-based carbonic anhydrase inhibitors: insight into CAII/CAIX specificity from a high-resolution crystal structure, modeling, and quantum chemical calculations.
    BioMed Research International. Roč. 2014, Sept 18 (2014), 389869/1-389869/9. ISSN 2314-6133. E-ISSN 2314-6141
    R&D Projects: GA TA ČR(CZ) TE01020028; GA ČR GBP208/12/G016
    Institutional support: RVO:61388980 ; RVO:68378050 ; RVO:61388963
    Keywords : Drug design * Identification * Accuracy
    Subject RIV: EB - Genetics ; Molecular Biology
    Impact factor: 1.579, year: 2014

    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.
    Permanent Link: http://hdl.handle.net/11104/0243235


    Research data: RSC publishing
     
     
Number of the records: 1  

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