Linked Life Data

15448619

Source:http://linkedlifedata.com/resource/pubmed/id/15448619

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-9-27
pubmed:abstractText
Alpha-crystallin, a hetero-oligomer of alphaA- and alphaB-crystallin, is involved in maintaining eye lens transparency, primarily by its structural packing and chaperone activity. alphaA- and alphaB-crystallin share significant sequence homology, which is almost exclusively restricted to the central, conserved "alphaA-crystallin domain". The flanking N-terminal domain and C-terminal extension are highly variable both in sequence and length. Mutations and age-related post-translational modifications of these proteins are associated with congenital and age-onset cataracts. Interestingly, most mutations or truncations in the C-terminal extensions of the alpha-crystallins and other alpha-sHsps like Hsp27 lead to pathology. It is therefore important to understand the structure/function relationship of this region. Sequence alignment of the C-terminal extensions of alphaA- and alphaB-crystallin with other homologues shows a conserved IXI/V motif. The purpose of this study was to investigate the role of this conserved motif, IPV in alphaA-crystallin and IPI in alphaB-crystallin (corresponding to residues 159-161 in both crystallins), in the structure and chaperone activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1090-0535
pubmed:author
pubmed:issnType
Electronic
pubmed:day
8
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
655-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies.
pubmed:affiliation
Center for Cellular and Molecular Biology, Hyderabad, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't