title: Structure of the sodium channel pore revealed by serial cysteine mutagenesis.
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.
authors.affiliation: Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: M T
authors.initials: MT
authors.lastname: Pérez-García
authors.forename: N
authors.initials: N
authors.lastname: Chiamvimonvat
authors.forename: E
authors.initials: E
authors.lastname: Marban
authors.forename: G F
authors.initials: GF
authors.lastname: Tomaselli
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002104:Cadmium / Q000494:pharmacology; D003545:Cysteine / Q000737:chemistry; D015640:Ion Channel Gating / Q000187:drug effects; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009865:Oocytes; D017433:Protein Structure, Secondary; D051381:Rats; D015222:Sodium Channels / Q000737:chemistry* / Q000187:drug effects; D013329:Structure-Activity Relationship; D013779:Tetrodotoxin / Q000494:pharmacology; D014982:Xenopus laevis
chemical_list: D015222:Sodium Channels; D002104:Cadmium; D013779:Tetrodotoxin; D003545:Cysteine