Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-7-29
pubmed:abstractText
Five inhibitors (PLI-I-V) against Trimeresurus flavoviridis (Tf, habu snake, Crotalinae) venom phospholipase A2 (PLA2) isozymes have been isolated from its serum. PLI-I, which is composed of two repeated three-finger motifs, and PLI-IV and PLI-V, which contain a sequence similar to the carbohydrate recognition domain (CRD) of C-type lectins, were expressed in the forms fused with glutathione S-transferase (GST). The resulting GST-PLIs showed ability to bind to three Tf venom PLA2 isozymes. The binding study with the truncated forms indicated that one of two three-finger motifs of PLI-I was able to bind to PLA2 isozymes. The N-terminal 37-amino acid fragment and the CRD-like domain of PLI-IV and PLI-V were bound to PLA2 isozymes. On the other hand, their C-terminal 12-amino acid segment also associated with PLA2 isozymes. When either of two units of a hydrophobic tripeptide in this sequence was replaced by trialanine, the binding was completely abolished, indicating that the C-terminal hydrophobic cores of PLI-IV and PLI-V were critically responsible for the binding to venom PLA2 isozymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
429
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
385-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Structural elements of Trimeresurus flavoviridis serum inhibitors for recognition of its venom phospholipase A2 isozymes.
pubmed:affiliation
Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't