Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-1-18
pubmed:abstractText
Structure-function studies have identified key functional motifs in the acetylcholine receptor, including residues that contribute to the ion channel and to the ligand-binding sites. Little is known, however, about determinants of channel gating kinetics. To identify structural correlates of gating, we examined the structural basis of the fetal-to-adult decrease in channel open time conferred by the presence of the epsilon subunit in place of the gamma subunit. By constructing chimeras composed of segments of the epsilon and gamma subunits, we show that the main determinant of this kinetic change is a 30 residue segment of a predicted amphipathic helix located between transmembrane domains M3 and M4. Further subdividing the amphipathic helix revealed that either multiple residues or its overall conformation confers this regulation of channel kinetics. We also show that L440 and M442, conserved residues within M4 of the gamma subunit, contribute to long duration openings characteristic of the fetal receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1395-402
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7993630-Amino Acid Sequence, pubmed-meshheading:7993630-Animals, pubmed-meshheading:7993630-Electric Conductivity, pubmed-meshheading:7993630-Fetus, pubmed-meshheading:7993630-Humans, pubmed-meshheading:7993630-Ion Channel Gating, pubmed-meshheading:7993630-Kinetics, pubmed-meshheading:7993630-Membrane Proteins, pubmed-meshheading:7993630-Mice, pubmed-meshheading:7993630-Molecular Sequence Data, pubmed-meshheading:7993630-Mutagenesis, Site-Directed, pubmed-meshheading:7993630-Patch-Clamp Techniques, pubmed-meshheading:7993630-Protein Structure, Secondary, pubmed-meshheading:7993630-Receptors, Nicotinic, pubmed-meshheading:7993630-Recombinant Fusion Proteins, pubmed-meshheading:7993630-Sequence Alignment, pubmed-meshheading:7993630-Sequence Homology, Amino Acid, pubmed-meshheading:7993630-Structure-Activity Relationship
pubmed:year
1994
pubmed:articleTitle
Structural basis of the different gating kinetics of fetal and adult acetylcholine receptors.
pubmed:affiliation
Department of Physiology and Biophysics, Mayo Foundation, Rochester, Minnesota 55905.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.