Linked Life Data

15664174

Source:http://linkedlifedata.com/resource/pubmed/id/15664174

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-1-24
pubmed:abstractText
Acquisition of secondary, tertiary, and quaternary structure is critical to the fabrication, assembly, and function of ion channels, yet the relationship between these biogenic events remains unclear. We now address this issue in voltage-gated K(+) channels (Kv) for the T1 domain, an N-terminal Kv recognition domain that is responsible for subfamily-specific, efficient assembly of Kv subunits. This domain forms a 4-fold symmetric tetramer. We have identified residues along the axial T1-T1 interface that are critical for tertiary and quaternary structure, shown that mutations at one end of the axial T1 interface can perturb the crosslinking of an intersubunit cysteine pair at the other end, and demonstrated that tertiary folding and tetramerization of this Kv domain are coupled. A threshold level of tertiary folding is required for monomers to oligomerize. Coupling between tertiary and quaternary structure formation may be a common feature in the biogenesis of multimeric proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Coupled tertiary folding and oligomerization of the T1 domain of Kv channels.
pubmed:affiliation
Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't