Linked Life Data

21554249

Source:http://linkedlifedata.com/resource/pubmed/id/21554249

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-7-13
pubmed:abstractText
Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3-3? isoform is a molecular chaperone, preventing the stress-induced aggregation of target proteins in a manner comparable with that of the unrelated sHsps (small heat-shock proteins). 1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3? and is similar in structure and length to the C-terminal extension of mammalian sHsps. The extension stabilizes 14-3-3?, but has no direct role in chaperone action. Lys(49) is an important functional residue within the ligand-binding groove of 14-3-3? with K49E 14-3-3? exhibiting markedly reduced binding to phosphorylated and non-phosphorylated ligands. The R18 peptide binds to the binding groove of 14-3-3? with high affinity and also reduces the interaction of 14-3-3? ligands. However, neither the K49E mutation nor the presence of the R18 peptide affected the chaperone activity of 14-3-3?, implying that the C-terminal extension and binding groove of 14-3-3? do not mediate interaction with target proteins during chaperone action. Other region(s) in 14-3-3? are most likely to be involved, i.e. the protein's chaperone and phosphoserine-binding activities are functionally and structurally separated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1470-8728
pubmed:author
pubmed:copyrightInfo
© The Authors Journal compilation © 2011 Biochemical Society
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
437
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
493-503
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
NMR spectroscopy of 14-3-3? reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3?.
pubmed:affiliation
School of Chemistry and Physics, The University of Adelaide, Adelaide, SA 5005, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't