Voltage-gated Na+ channel, NavCh. 3d-structure known (3ROW; Payandeh et al., 2011). An anionic coordination site was proposed to confer Na+ selectivity through partial dehydration of Na+ via its direct interaction with conserved glutamate side chains. The pore is preferentially occupied by two ions, which can switch between different configurations by crossing low free-energy barriers (Furini and Domene, 2012). Jiang et al. 2018 presented high-resolution structures of NavAb with the analogous gating-charge mutations that have similar functional effects as in the human channels that cause hypokalaemic and normokalaemic periodic paralysis.
(see TC#s 1.A.1.10.4 and 1.A.1.11.32).
|Protein Name:||Ion transport protein|
|Species:||Arcobacter butzleri (strain RM4018)  |
|Number of TMSs:||5|
1: MYLRITNIVE SSFFTKFIIY LIVLNGITMG LETSKTFMQS FGVYTTLFNQ IVITIFTIEI
61: ILRIYVHRIS FFKDPWSLFD FFVVAISLVP TSSGFEILRV LRVLRLFRLV TAVPQMRKIV
121: SALISVIPGM LSVIALMTLF FYIFAIMATQ LFGERFPEWF GTLGESFYTL FQVMTLESWS
181: MGIVRPLMEV YPYAWVFFIP FIFVVTFVMI NLVVAIIVDA MAILNQKEEQ HIIDEVQSHE
241: DNINNEIIKL REEIVELKEL IKTSLKN