Linked Life Data

9292731

Source:http://linkedlifedata.com/resource/pubmed/id/9292731

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-10-16
pubmed:abstractText
We have examined domain interactions in the rod cyclic nucleotide-gated ion channel using both physiological and biochemical interaction assays. We have found an interaction between two regions of the channel distant in primary structure, the amino-terminal region and the carboxyl-terminal region containing the cyclic nucleotide-binding (CNB) domain. The interaction in functional channels was detected by the formation of a disulfide bond between cysteine residues at position 35 in the amino-terminal region and 481 in the carboxyl-terminal region. The disulfide bond resulted in channel potentiation, which was due, in part, to an increase in availability of C481 to modification when the channels were open. This state dependence is likely to underlie previously reported potentiation of cyclic nucleotide-gated channels by sulfhydryl-reactive compounds. Polypeptides derived from the amino-terminal and carboxyl-terminal regions were shown to interact, even under conditions which precluded disulfide bond formation. These data argue for a previously unknown, direct interaction between disparate regions of channel sequence.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-41
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Direct interaction between amino- and carboxyl-terminal domains of cyclic nucleotide-gated channels.
pubmed:affiliation
Department of Physiology and Biophysics, Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't