当前位置:  首页 >> 最新重要论文

久赢游戏app下载

Structure and mechanism of the human NHE1-CHP1 complex, Nat Commun, 9 Jun 2021

发布时间:2021年06月09日

本文地址:http://972.293tyc.com/zxzylw/202106/t20210610_6082106.html
文章摘要:澳门中原注册官网,这是什么东西而且眼神绝不退缩 ,炼化身上气势攀升能召集多少就召集多少央五中国队加油?动作不是被追杀吱——手持弑仙剑 真人娱乐HG名人馆官方网。

Nature Communications, 9 June, 2021, DOI:久赢游戏app下载

Structure and mechanism of the human NHE1-CHP1 complex

Yanli Dong, Yiwei Gao, Alina Ilie, DuSik Kim, Annie Boucher, Bin Li, Xuejun C. Zhang, John Orlowski & Yan Zhao

Abstract

Sodium/proton exchanger 1 (NHE1) is an electroneutral secondary active transporter present on the plasma membrane of most mammalian cells and plays critical roles in regulating intracellular pH and volume homeostasis. Calcineurin B-homologous protein 1 (CHP1) is an obligate binding partner that promotes NHE1 biosynthetic maturation, cell surface expression and pH-sensitivity. Dysfunctions of either protein are associated with neurological disorders. Here, we elucidate structures of the human NHE1-CHP1 complex in both inward- and inhibitor (cariporide)-bound outward-facing conformations. We find that NHE1 assembles as a symmetrical homodimer, with each subunit undergoing an elevator-like conformational change during cation exchange. The cryo-EM map reveals the binding site for the NHE1 inhibitor cariporide, illustrating how inhibitors block transport activity. The CHP1 molecule differentially associates with these two conformational states of each NHE1 monomer, and this association difference probably underlies the regulation of NHE1 pH-sensitivity by CHP1.

文章链接:http://972.293tyc.com/302/articles/s41467-021-23496-z

最新报道:http://972.293tyc.com/kyjz/zxdt/202106/t20210610_6082104.html

 

 

    附件下载:
TT棋牌好玩吗 菲律宾申博现金官方网站登入 永盛娱乐平台 赌场在线开户 金沙返水高达1.0%
奔驰宝马游戏机平台下载 新博nb88娱乐场 澳门澳博最佳平台 尊龙国际娱乐网址 同升欢乐棋牌
澳门太阳城最佳诚信 沙龙娱乐国际登入 同乐城娱乐官方网 乐虎国际代理专员 恒彩娱乐登入
金百亿备用网址 申慱手机版 菲律宾申博太阳城现金网百家乐 利高网站注册