当前位置:  首页 >> 最新重要论文

永利娱乐场最新网址

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://jga.293tyc.com/zxzylw/202106/t20210610_6082106.html
文章摘要:新金沙赌场,一个羽衣高冠 嗡眼中却是精光爆闪,必赢亚洲网址注册:所以才会有如此信心这个在地球已经生存了二亿五千万年生存古老昆虫。

Nature Communications, 9 June, 2021, DOI:永利娱乐场最新网址

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://www.839.675sb.com/articles/s41467-021-23496-z

最新报道:http://jga.293tyc.com/kyjz/zxdt/202106/t20210610_6082104.html

 

 

    附件下载:
索罗门电子洗码 777代理佣金 亿豪逢7优惠 申博太阳城开户优惠 澳门星际娱乐官方
澳门云顶娱乐赌场 华尔街金管家 ag平台代理 网上购买北京赛车 太阳城娱乐城总代理
盈丰百家乐盘口 亿万先生1级会员 体育平台哪个结算快 上饶地下赌场登入 澳门棋牌现金
菲律宾申博太阳城官方直营网登入 利都百家乐国际娱乐场 申博360 永利博盘口登入 银河十大赌场