Linked Life Data

17548059

Source:http://linkedlifedata.com/resource/pubmed/id/17548059

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-6-18
pubmed:abstractText
Among four subtypes of mammalian HCN channels, HCN1 has the fastest activation and deactivation kinetics while HCN4 shows the slowest. We previously showed that the activation kinetics are determined mainly by S1, S1-S2, and the S6-cyclic nucleotide binding domain. However, the effects of those regions on the deactivation kinetics were relatively small. Therefore, we investigated the structural basis for deactivation kinetics. Substitution of the core region (from S3 to S6) between HCN1 and HCN4 did not affect deactivation kinetics. This suggests that the peripheral regions (outside of S3 to S6) determine subtype-specific deactivation kinetics. Furthermore, we examined whether peripheral regions determined the deactivation kinetics across species by introducing the core region of DMIH (Drosophila homologue) into both HCN1 and HCN4. The DMIH core with HCN1 activated and deactivated more than threefold faster than that with HCN4. Taken together, the peripheral domains are diversified to create distinct kinetics.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
359
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
592-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Peripheral N- and C-terminal domains determine deactivation kinetics of HCN channels.
pubmed:affiliation
Department of Physiology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't