北京大学 | ENGLISH
讲座信息
Revealing Auto-inhibition And Activation Mechanism of Human Dynein-1
日期: 2017-02-10       点击量: 528
IMM膜蛋白结构研究室 学术报告 
题目:Revealing Auto-inhibition And Activation Mechanism of Human Dynein-1
报告人:Kai Zhang, Ph.D.
MRC Laboratory of Molecular Biology, UK
时间:2017年2月21日(星期二)下午3:00-4:30
地点:北京大学英杰交流中心306会议室
Host:北京大学分子医学研究所 陈雷 (Tel. 6275-5557)
摘要: Cytoplasmic dynein-1 binds dynactin in the presence of cargo adaptor proteins to form a transport machine capable of long distance processive movement along microtubules. However, it is unclear why human dynein-1 cannot move on its own and how dynactin activates movement. Here we present a cryo-electron microscopy (cryo-EM) structure of the complete 1.4 MDa human dynein-1 complex in an inhibited conformation known as the phi-particle. We reveal the 3D structure of the cargo binding dynein tail and show how self-dimerization of the motor-domains locks them in a conformation with low microtubule affinity. Disrupting dimerization with structure-based mutagenesis drives dynein-1 into an open-form with higher affinity for both microtubules and dynactin. We find the open-form is also inhibited for movement and that dynactin relieves this by reorienting the motor domains to interact correctly with microtubules. Our model explains how dynactin binding to the dynein-1 tail stimulates its motor activity directly.
欢迎各位老师同学积极参加!
[友情链接]
北大生科微信公众号 生声不息微信公众号
联系我们 | 地理位置
北京大学生命科学学院 版权所有 地址:北京市海淀区颐和园路5号金光生命科学大楼