4qiz: Difference between revisions
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==Crystal structure of human carbonic anhydrase isozyme XIII with inhibitor== | ==Crystal structure of human carbonic anhydrase isozyme XIII with inhibitor== | ||
<StructureSection load='4qiz' size='340' side='right' caption='[[4qiz]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='4qiz' size='340' side='right' caption='[[4qiz]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qiy|4qiy]], [[4qj0|4qj0]], [[4qjm|4qjm]], [[4qjo|4qjo]], [[4qjp|4qjp]], [[4qjw|4qjw]], [[4qjx|4qjx]], [[4qtl|4qtl]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qiy|4qiy]], [[4qj0|4qj0]], [[4qjm|4qjm]], [[4qjo|4qjo]], [[4qjp|4qjp]], [[4qjw|4qjw]], [[4qjx|4qjx]], [[4qtl|4qtl]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qiz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qiz RCSB], [http://www.ebi.ac.uk/pdbsum/4qiz PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qiz OCA], [http://pdbe.org/4qiz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qiz RCSB], [http://www.ebi.ac.uk/pdbsum/4qiz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qiz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4qiz" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:24, 18 January 2017
Crystal structure of human carbonic anhydrase isozyme XIII with inhibitorCrystal structure of human carbonic anhydrase isozyme XIII with inhibitor
Structural highlights
Function[CAH13_HUMAN] Reversible hydration of carbon dioxide. Publication Abstract from PubMedSubstituted tri- and tetrafluorobenzenesulfonamides were designed, synthesized, and evaluated as high-affinity and isoform-selective carbonic anhydrase (CA) inhibitors. Their binding affinities for recombinant human CA I, II, VA, VI, VII, XII, and XIII catalytic domains were determined by fluorescent thermal shift assay, isothermal titration calorimetry, and a stopped-flow CO2 hydration assay. Variation of the substituents at the 2-, 3-, and 4-positions yielded compounds with a broad range of binding affinities and isoform selectivities. Several 2,4-substituted-3,5,6-trifluorobenzenesulfonamides were effective CA XIII inhibitors with high selectivity over off-target CA I and CA II. 3,4-Disubstituted-2,5,6-trifluorobenzenesulfonamides bound CAs with higher affinity than 2,4-disubstituted-3,5,6-trifluorobenzenesulfonamides. Many such fluorinated benzenesulfonamides were found to be nanomolar inhibitors of CA II, CA VII, tumor-associated CA IX and CA XII, and CA XIII. X-ray crystal structures of inhibitors bound in the active sites of several CA isoforms provide structure-activity relationship information for inhibitor binding affinities and selectivity. Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties toward Carbonic Anhydrases.,Dudutiene V, Zubriene A, Smirnov A, Timm DD, Smirnoviene J, Kazokaite J, Michailoviene V, Zaksauskas A, Manakova E, Grazulis S, Matulis D ChemMedChem. 2015 Apr;10(4):662-87. doi: 10.1002/cmdc.201402490. Epub 2015 Mar, 10. PMID:25758852[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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