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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
1997-1-16
|
| pubmed:abstractText |
Phospholipases A2 (PLA2) are widely distributed in nature and are well characterized proteins with respect to their catalytic and pharmacological activities. A wealth of structural information has recently become available both from X-ray diffraction and NMR studies, and although a detailed model of the catalytic mechanism of PLA2 has been proposed, the structural bases of other aspects of PLA2 function, such as interfacial activation and venom PLA2 pharmacological activities, are still under debate. An appreciation of the PLA2 protein structure will yield new insights with regard to these activities. The salient structural features of the class I, II and III PLA2 are discussed with respect to their functional roles.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0041-0101
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
34
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
827-41
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1996
|
| pubmed:articleTitle |
Phospholipase A2--a structural review.
|
| pubmed:affiliation |
Department of Physics, IBILCE/UNESP, São Jose do Rio Preto, Brazil.
|
| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|