Recent progress on the structure and function of the TrkH/KtrB ion channel

被引：21

作者：

Levin, Elena J. ^{[1
]}

Zhou, Ming ^{[1
]}

机构：

[1] Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2014年 / 27卷

基金：

美国国家卫生研究院;

关键词：

K+-UPTAKE SYSTEM; MEMBRANE REGION M-2C2; ESCHERICHIA-COLI; POTASSIUM CHANNEL; GLYCINE RESIDUES; KTRAB SYSTEM; PROTEIN TRKA; GATING RING; RCK DOMAIN; SELECTIVITY;

D O I：

10.1016/j.sbi.2014.06.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Members of the Superfamily of K+ Transporters (SKT) are integral membrane proteins that mediate the uptake of ions into non-animal cells. Although these proteins are homologous to the well-characterized K+ channel family, relatively little was known about their transport and gating mechanisms until the recent determination of crystal structures for two SKT proteins, TrkH and KtrB. These structures reveal that the SKT proteins are channels, containing a flexible loop in the middle of the permeation pathway that may act as a gate. Two different conformational changes have been observed for the associated gating rings, suggesting different mechanisms of regulation by the binding of nucleotides.

引用

页码：95 / 101

页数：7

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