The structure of full length human dynein-1 and the activation mechanism
讲座名称：
The structure of full length human dynein-1 and the activation mechanism
讲座时间：
2016-07-12
讲座人：
张凯
形式：
校区：
兴庆校区
实践学分：
讲座内容：
报告题目：The structure of full length human dynein-1 and the activation mechanism
报 告 人：张凯博士，剑桥MRC分子生物学实验室博士后
报告时间：2016年7月12日（星期二）上午11:15-12:00
报告地点：中一楼3113
报告摘 要：
Human cytoplasmic dynein-1 is a 1.4 MDa motor protein complex with 12 subunits, which transports many important cargos to the minus end of microtubules. However, it only becomes an efficient, unidirectional motor when bound to the gigantic essential co-factor dynactin and a cargo adaptor protein (BICD2). We reported the structure of the 23-subunit dynactin complex by cryo-electron microscopy at 4.0Å overall and tail/dynactin/BicD complex at 8.2Å. The assembly mechanism of dynactin and its interaction with dynein-1 were unambiguously revealed. Cryo-EM structure of a full length human dynein-1 in the state of compact Phi particle has been solved to high resolution. All subunits have been identified from the 8Å map of dynein-1 tail with most helices built. The 3.8Å motor domain shows how dynein is auto-inhibited via dimerization. Key residues were identified in the interface. Mutagenesis revealed how these residues affect dimerization and processivity of dynein-1. A detailed activation mechanism has been proposed based on functional study and dynamic structural analysis of dynein-1 in Phi particle, open dynein alone and open dynein in dynein/dynactin/BicD (DDB) complex.
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