Linked Life Data

8738208

Source:http://linkedlifedata.com/resource/pubmed/id/8738208

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-10-24
pubmed:databankReference
pubmed:abstractText
We have recently determined the first crystal structure of a theta class glutathione transferase. We have aligned the amino acid sequences of members of the family using the crystal structure as a guide. The alignment has revealed a consensus pattern of residues that first identifies a protein as belonging to the glutathione transferase superfamily, and second is able to distinguish theta class members from other classes of glutathione transferases. The consensus residues unique to the theta class are found to cluster mostly on the hydrophilic surface and flanking loops of helix 2, a region found to be structurally diverse amongst crystal structures of the different glutathione transferase classes. When the consensus pattern was scanned against sequence databases, a number of matches were made with proteins not formally identified as glutathione transferases. Some of these matches indicated that several stress-related proteins belong to the theta class GST family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
A structurally derived consensus pattern for theta class glutathione transferases.
pubmed:affiliation
Ian Potter Foundation Protein Crystallography Laboratory, St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't