Linked Life Data

12354605

Source:http://linkedlifedata.com/resource/pubmed/id/12354605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-9-30
pubmed:abstractText
Chaperonins are large oligomers made up of two superimposed rings, each enclosing a cavity used for the folding of other proteins. Among the chaperonins, the eukaryotic cytosolic chaperonin CCT is the most complex, not only with regard to its subunit composition but also with respect to its function, still not well understood. Unlike the more well studied eubacterial chaperonin GroEL, which binds any protein that presents stretches of hydrophobic residues, CCT recognises in its substrates specific binding determinants and interacts with them through particular combinations of CCT subunits. Folding then occurs after the conformational changes induced in the chaperonin upon nucleotide binding have occurred, through a mechanism that, although still poorly defined, clearly differs from the one established for GroEL. Although CCT seems to be mainly involved in the folding of actin and tubulin, other substrates involved in various cellular roles are beginning to be characterised, including many WD40-repeat, 7-blade propeller proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
529
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.
pubmed:affiliation
Centro Nacional de Biotecnologi;a, C.S.I.C., Campus Universidad Autónoma de Madrid, 28049, Madrid, Spain. jmv@cnb.uam.es
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't