Linked Life Data

10591065

Source:http://linkedlifedata.com/resource/pubmed/id/10591065

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1999-12-23
pubmed:abstractText
The role of two cysteine residues--Cys122 and Cys154--in the structure of the strong inward rectifier K+ channel, Kir2.1, has been investigated using site-directed mutagenesis and electrophysiology. Such cysteine residues are conserved across the inward rectifier family and may be expected to form a crucial disulphide bond. Our experiments show that when the cysteines are absent, the protein is expressed, but the channels are not functional, suggesting that the disulphide bond is essential for correct channel assembly. However, reducing agents applied extracellularly have little effect on current amplitude in wild-type, so that, once the channel is assembled correctly in the membrane, the disulphide bonds are no longer essential for function. Molecular modelling suggests that a disulphide bond is formed--this may be either an intra- or an inter-subunit.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0031-6768
pubmed:author
pubmed:issnType
Print
pubmed:volume
438
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
778-81
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
The possible role of a disulphide bond in forming functional Kir2.1 potassium channels.
pubmed:affiliation
Centre for the Mechanisms of Human Toxicity, University of Leicester, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't