Structural basis for the interaction between carbonic anhydrase and 1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamides
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21395315
DOI
10.1021/jm2000213
Knihovny.cz E-resources
- MeSH
- Carbonic Anhydrase Inhibitors chemistry metabolism pharmacology MeSH
- Isoquinolines chemistry metabolism pharmacology MeSH
- Isoenzymes antagonists & inhibitors chemistry metabolism MeSH
- Carbonic Anhydrase II antagonists & inhibitors chemistry metabolism MeSH
- Protein Conformation MeSH
- Crystallography, X-Ray MeSH
- Humans MeSH
- Models, Molecular MeSH
- Substrate Specificity MeSH
- Protein Binding MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Carbonic Anhydrase Inhibitors MeSH
- Isoquinolines MeSH
- Isoenzymes MeSH
- Carbonic Anhydrase II MeSH
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.
References provided by Crossref.org
4-Sulfamoylphenylalkylamides as Inhibitors of Carbonic Anhydrases Expressed in Vibrio cholerae
