A mutation in segment IVS6 disrupts fast inactivation of sodium channels

Authors :: McPhee, Jancy C.
Ragsdale, David S.
Scheuer, Todd
Catterall, William A.
Source :: Proceedings of the National Academy of Sciences of the United States. Dec 6, 1994, Vol. 91 Issue 25, p12346, 5 p.
Publication Year :: 1994
Abstract: Site-directed mutagenetic studies of the transmembrane segment S6 of domain IV (IVS6) in the sodium ion-channel reveals that the intracellular end of this segment contributes to fast channel inactivation. This segment is present in the hydrophobic receptor site for the fast inactivation gate. The entry to and stability of the inactivated state are maintained by three hydrophobic amino acid residues at sites 1774-1776 in the IVS6 segment.

Subjects :: Sodium channels -- Research
Mutation (Biology) -- Analysis
Structure-activity relationships (Biochemistry) -- Analysis
Science and technology

ISSN :: 00278424
Volume :: 91
Issue :: 25
Database :: Gale General OneFile
Journal :: Proceedings of the National Academy of Sciences of the United States
Publication Type :: Academic Journal
Accession number :: edsgcl.16569649

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