Source:http://linkedlifedata.com/resource/pubmed/id/14660577
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2004-2-17
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| pubmed:databankReference | |
| pubmed:abstractText |
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.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/carbonic anhydrase XIV
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
20
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| pubmed:volume |
279
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
7223-8
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14660577-Amino Acid Sequence,
pubmed-meshheading:14660577-Animals,
pubmed-meshheading:14660577-Binding Sites,
pubmed-meshheading:14660577-COS Cells,
pubmed-meshheading:14660577-Calibration,
pubmed-meshheading:14660577-Carbonic Anhydrases,
pubmed-meshheading:14660577-Catalysis,
pubmed-meshheading:14660577-Catalytic Domain,
pubmed-meshheading:14660577-Cell Membrane,
pubmed-meshheading:14660577-Crystallography, X-Ray,
pubmed-meshheading:14660577-DNA, Complementary,
pubmed-meshheading:14660577-Humans,
pubmed-meshheading:14660577-Ions,
pubmed-meshheading:14660577-Mice,
pubmed-meshheading:14660577-Mice, Inbred C57BL,
pubmed-meshheading:14660577-Models, Molecular,
pubmed-meshheading:14660577-Molecular Sequence Data,
pubmed-meshheading:14660577-Protein Conformation,
pubmed-meshheading:14660577-Protein Isoforms,
pubmed-meshheading:14660577-Protein Structure, Tertiary,
pubmed-meshheading:14660577-Sequence Homology, Amino Acid,
pubmed-meshheading:14660577-Zinc
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| pubmed:year |
2004
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| pubmed:articleTitle |
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes.
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| pubmed:affiliation |
Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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