Linked Life Data

19467292

Source:http://linkedlifedata.com/resource/pubmed/id/19467292

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2009-7-6
pubmed:abstractText
Selenocysteine (Sec) is co-translationally incorporated into selenoproteins at a reprogrammed UGA codon. In mammals, this requires a dedicated machinery comprising a stem-loop structure in the 3' UTR RNA (the SECIS element) and the specific SECIS Binding Protein 2. In this report, disorder-prediction methods and several biophysical techniques showed that ca. 70% of the SBP2 sequence is disordered, whereas the RNA binding domain appears to be folded and functional. These results are consistent with a recent report on the role of the Hsp90 chaperone for the folding of SBP2 and other functionally unrelated proteins bearing an RNA binding domain homologous to SBP2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1638-6183
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1003-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein.
pubmed:affiliation
Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, IBMC, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't