Linked Life Data

6835368

Source:http://linkedlifedata.com/resource/pubmed/id/6835368

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5906
pubmed:dateCreated
1983-5-5
pubmed:databankReference
pubmed:abstractText
A 23,000 molecular weight beta-crystallin (beta 23) of the murine eye lens is encoded in a 4.1 +/- 0.3-kilobase gene containing three introns. Each of the four exons seems to code for a separate structural motif of the protein, whose tertiary structure was predicted by an interactive computer graphics technique based on the crystallographic structure of bovine gamma II-crystallin. The first exon also encodes a hydrophobic N-terminal peptide resembling membrane anchor sequences of other proteins. Our results indicate structural homology among the beta- and gamma-crystallin polypeptides, and link gene structure with protein structure in this superfamily of lens proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
310-5
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
Gene and protein structure of a beta-crystallin polypeptide in murine lens: relationship of exons and structural motifs.
pubmed:publicationType
Journal Article, Comparative Study