北京快乐8玩法

当前位置:   首页 >> 最新重要论文

最新重要论文

Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function, PNAS, 20 Mar 2020

发布时间: 2020年03月20日

PNAS, 20 March, 2020, DOI:

Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function

si wu, liu hong, yuqing wang, jieqiong yu, jie yang, jie yang, hong zhang, and sarah perrett

Abstract

北京快乐8玩法hsp70 is a conserved molecular chaperone that plays an indispensable role in regulating protein folding, translocation, and degradation. the conformational dynamics of hsp70 and its regulation by cochaperones are vital to its function. using bulk and single-molecule fluorescence resonance energy transfer (smfret) techniques, we studied the interdomain conformational distribution of human stress-inducible hsp70a1 and the kinetics of conformational changes induced by nucleotide and the hsp40 cochaperone hdj1. we found that the conformations between and within the nucleotide- and substrate-binding domains show heterogeneity. the conformational distribution in the atp-bound state can be induced by hdj1 to form an “adp-like” undocked conformation, which is an atpase-stimulated state. kinetic measurements indicate that hdj1 binds to monomeric hsp70 as the first step, then induces undocking of the two domains and closing of the substrate-binding cleft. dimeric hdj1 then facilitates dimerization of hsp70 and formation of a heterotetrameric hsp70–hsp40 complex. our results provide a kinetic view of the conformational cycle of hsp70 and reveal the importance of the dynamic nature of hsp70 for its function.

文章链接:  

相关报道: http://smic-snaps.com/kyjz/zxdt/202003/t20200322_5518040.html

 

 

    附件下载:
北京快乐8_北京快乐8玩法|官网 快乐赛车_快乐赛车网址|官网 极速赛车_极速赛车pk10|信誉平台 MC赛车|首页 秒速飞艇_秒速飞艇彩票|信誉平台 极速快三_极速快三平台|正规授权 快3_快3平台|信誉平台 快乐赛车|信誉平台 幸运快3_幸运快3彩票|首页 幸运快三_幸运快三平台|官方平台 加拿大时时彩_加拿大时时彩软件|正规授权