6qqm: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6qqm is ON HOLD
+==Crystal structure of the alpha carbonic anhydrase from Schistosoma mansoni==
+<StructureSection load='6qqm' size='340' side='right'caption='[[6qqm]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6qqm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QQM FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qqm OCA], [https://pdbe.org/6qqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qqm RCSB], [https://www.ebi.ac.uk/pdbsum/6qqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qqm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A3Q0KSG2_SCHMA A0A3Q0KSG2_SCHMA] Reversible hydration of carbon dioxide.[RuleBase:RU367011]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Tegumental carbonic anhydrase from the worm Schistosoma mansoni (SmCA) is considered a new anti-parasitic target because suppressing its expression interferes with schistosome metabolism and virulence. Here, we present the inhibition profiles of selenoureido compounds on recombinant SmCA and resolution of the first X-ray crystal structures of SmCA in adduct with a selection of such inhibitors. The key molecular features of such compounds in adduct with SmCA were obtained and compared to the human isoform hCA II, in order to understand the main structural factors responsible for enzymatic affinity and selectivity. Compounds that more specifically inhibited the schistosome versus human enzymes were identified. The results expand current knowledge in the field and pave the way for the development of more potent antiparasitic agents in the near future.
-Authors:
+Structural Insights into Schistosoma mansoni Carbonic Anhydrase (SmCA) Inhibition by Selenoureido-Substituted Benzenesulfonamides.,Angeli A, Ferraroni M, Da'dara AA, Selleri S, Pinteala M, Carta F, Skelly PJ, Supuran CT J Med Chem. 2021 Jul 22;64(14):10418-10428. doi: 10.1021/acs.jmedchem.1c00840., Epub 2021 Jul 7. PMID:34232641<ref>PMID:34232641</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6qqm" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Schistosoma mansoni]]
+[[Category: Angeli A]]
+[[Category: Ferraroni M]]
+[[Category: Supuran CT]]