1rj6

<table><tr><td colspan='2'>[[1rj6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RJ6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA14, CAR14, CATM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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://proteopedia.org/fgij/fg.htm?mol=1rj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rj6 OCA], [http://pdbe.org/1rj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rj6 RCSB], [http://www.ebi.ac.uk/pdbsum/1rj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rj6 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CAH14_MOUSE CAH14_MOUSE]] Reversible hydration of carbon dioxide.

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== Publication Abstract from PubMed ==

Carbonic anhydrase (CA) XIV is the most recently identified mammalian carbonic anhydrase isozyme, and its presence has been demonstrated in a number of tissues. Full-length CA XIV is a transmembrane protein composed of an extracellular catalytic domain, a single transmembrane helix, and a short intracellular polypeptide segment. The amino acid sequence identity of human CA XIV relative to the other membrane-associated isozymes (CA IV, CA IX, and CA XII) is 34-46%. We report here the expression and purification of both the full-length enzyme and a truncated, secretory form of murine CA XIV. Both forms of this isozyme are highly active, and both show an abrogation of activity in the presence of 0.2% SDS, in contrast to the behavior of murine CA IV. We also report the crystal structure of the extracellular domain of murine CA XIV at 2.8 A resolution and of an enzyme-acetazolamide complex at 2.9 A resolution. The structure shows a monomeric glycoprotein with a topology similar to that of other mammalian CA isozymes. Based on the x-ray crystallographic results, we compare and contrast known structures of membrane-associated CA isozymes to rationalize the structural elements responsible for the SDS resistance of CA IV and to discuss prospects for the design of selective inhibitors of membrane-associated CA isozymes.

Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes.,Whittington DA, Grubb JH, Waheed A, Shah GN, Sly WS, Christianson DW J Biol Chem. 2004 Feb 20;279(8):7223-8. Epub 2003 Dec 3. PMID:14660577<ref>PMID:14660577</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rj6" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Carbonate dehydratase]]

[[Category: Lk3 transgenic mice]]

[[Category: Christianson, D W]]

[[Category: Grubb, J H]]

[[Category: Shah, G N]]

[[Category: Sly, W S]]

[[Category: Waheed, A]]

[[Category: Whittington, D A]]

[[Category: Zinc enzyme]]