3fe4: Difference between revisions
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New page: '''Unreleased structure''' The entry 3fe4 is ON HOLD Authors: Pilka, E.S., Kochan, G., Krysztofinska, E., Muniz, J., Yue, W.W., Roos, A.K., von Delft, F., Arrowsmith, C.H., Weigelt, J.,... |
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==Crystal Structure of Human Carbonic Anhydrase vi== | |||
<StructureSection load='3fe4' size='340' side='right'caption='[[3fe4]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fe4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FE4 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]] 1.9Å</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=MG:MAGNESIUM+ION'>MG</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=3fe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fe4 OCA], [https://pdbe.org/3fe4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fe4 RCSB], [https://www.ebi.ac.uk/pdbsum/3fe4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fe4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAH6_HUMAN CAH6_HUMAN] Reversible hydration of carbon dioxide. Its role in saliva is unknown. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Zn(2+)-dependent carbonic anhydrases (CA) catalyse the reversible hydration of carbon dioxide to bicarbonate and participate in diverse physiological processes, hence having manifold therapeutic potentials. Among the 15 human CAs with wide-ranging sub-cellular localisation and kinetic properties, CA VI is the only secretory isoform. The 1.9A crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. The active site cavity contains a cluster of non-conserved residues that may be involved in ligand binding and have significant implications for developing the next-generation of isoform-specific inhibitors. | |||
Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.,Pilka ES, Kochan G, Oppermann U, Yue WW Biochem Biophys Res Commun. 2012 Mar 16;419(3):485-9. Epub 2012 Feb 14. PMID:22366092<ref>PMID:22366092</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3fe4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith CH]] | |||
[[Category: Bountra C]] | |||
[[Category: Edwards A]] | |||
[[Category: Kochan G]] | |||
[[Category: Krysztofinska E]] | |||
[[Category: Muniz J]] | |||
[[Category: Oppermann U]] | |||
[[Category: Pilka ES]] | |||
[[Category: Roos AK]] | |||
[[Category: Weigelt J]] | |||
[[Category: Yue WW]] | |||
[[Category: Von Delft F]] | |||
Latest revision as of 18:29, 1 November 2023
Crystal Structure of Human Carbonic Anhydrase viCrystal Structure of Human Carbonic Anhydrase vi
Structural highlights
FunctionCAH6_HUMAN Reversible hydration of carbon dioxide. Its role in saliva is unknown. Publication Abstract from PubMedZn(2+)-dependent carbonic anhydrases (CA) catalyse the reversible hydration of carbon dioxide to bicarbonate and participate in diverse physiological processes, hence having manifold therapeutic potentials. Among the 15 human CAs with wide-ranging sub-cellular localisation and kinetic properties, CA VI is the only secretory isoform. The 1.9A crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. The active site cavity contains a cluster of non-conserved residues that may be involved in ligand binding and have significant implications for developing the next-generation of isoform-specific inhibitors. Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.,Pilka ES, Kochan G, Oppermann U, Yue WW Biochem Biophys Res Commun. 2012 Mar 16;419(3):485-9. Epub 2012 Feb 14. PMID:22366092[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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