Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-18659
Proc Natl Acad Sci U S A 1996 Jan 09;931:300-4.
Show Gene links Show Anatomy links

Structure of the sodium channel pore revealed by serial cysteine mutagenesis.

Pérez-García MT , Chiamvimonvat N , Marban E , Tomaselli GF .


???displayArticle.abstract???
The pores of voltage-gated cation channels are formed by four intramembrane segments that impart selectivity and conductance. Remarkably little is known about the higher order structure of these critical pore-lining or P segments. Serial cysteine mutagenesis reveals a pattern of side-chain accessibility that contradicts currently favored structural models based on alpha-helices or beta-strands. Like the active sites of many enzymes of known structure, the sodium channel pore consists of irregular loop regions.

???displayArticle.pubmedLink??? 8552626
???displayArticle.pmcLink??? PMC40226
???displayArticle.link??? Proc Natl Acad Sci U S A



References [+] :
Akabas, Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit. 1994, Pubmed, Xenbase