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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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FE4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3fe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fe4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fe4 RCSB], [http://www.ebi.ac.uk/pdbsum/3fe4 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
==See Also== | ==See Also== | ||
*[[Carbonic anhydrase|Carbonic anhydrase]] | *[[Carbonic anhydrase|Carbonic anhydrase]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Arrowsmith, C H | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C | [[Category: Bountra, C]] | ||
[[Category: Delft, F von | [[Category: Delft, F von]] | ||
[[Category: Edwards, A | [[Category: Edwards, A]] | ||
[[Category: Kochan, G | [[Category: Kochan, G]] | ||
[[Category: Krysztofinska, E | [[Category: Krysztofinska, E]] | ||
[[Category: Muniz, J | [[Category: Muniz, J]] | ||
[[Category: Oppermann, U | [[Category: Oppermann, U]] | ||
[[Category: Pilka, E S | [[Category: Pilka, E S]] | ||
[[Category: Roos, A K | [[Category: Roos, A K]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Weigelt, J | [[Category: Weigelt, J]] | ||
[[Category: Yue, W W | [[Category: Yue, W W]] | ||
[[Category: Carbonic anhydrase]] | [[Category: Carbonic anhydrase]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
| Line 37: | Line 46: | ||
[[Category: Secretion]] | [[Category: Secretion]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
Revision as of 21:50, 21 December 2014
Crystal Structure of Human Carbonic Anhydrase viCrystal Structure of Human Carbonic Anhydrase vi
Structural highlights
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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