Linked Life Data

11375512

Source:http://linkedlifedata.com/resource/pubmed/id/11375512

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6
pubmed:dateCreated
2001-5-25
pubmed:abstractText
Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64% overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3(1)21 or P3(2)21 (unit-cell parameters a = 49.9, c = 271.8 A at 100 K) and the 1-4 isozyme in P4(1) or P4(3) (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
870-2
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Crystallization of two glutathione S-transferases from an unusual gene family.
pubmed:affiliation
Department of Pharmacology/Crystallography Centre, University of Western Australia and the Western Australian Institute for Medical Research, Nedlands WA 6907, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't