神经元中参与突触小泡融合的蛋白质结构。

Structure of proteins involved in synaptic vesicle fusion in neurons.

作者信息

Brunger A T

机构信息

The Howard Hughes Medical Institute and Department of Molecular and Cellular Physiology, Neurology and Neurological Sciences, and Stanford Synchrotron Radiation Laboratory, Stanford University, Stanford, California 94305, USA.

出版信息

Annu Rev Biophys Biomol Struct. 2001;30:157-71. doi: 10.1146/annurev.biophys.30.1.157.

DOI:10.1146/annurev.biophys.30.1.157

PMID:11340056

Abstract

The fusion of vesicles with target membranes is controlled by a complex network of protein-protein and protein-lipid interactions. Structures of the SNARE complex, synaptotagmin III, nSec1, domains of the NSF chaperone and its adaptor SNAP, and Rab3 and some of its effectors provide the framework for developing molecular models of vesicle fusion and for designing experiments to test these models.

摘要

囊泡与靶膜的融合由蛋白质-蛋白质和蛋白质-脂质相互作用的复杂网络控制。SNARE复合体、突触结合蛋白III、nSec1、NSF伴侣蛋白及其衔接蛋白SNAP的结构域，以及Rab3及其一些效应器的结构为开发囊泡融合分子模型和设计实验以测试这些模型提供了框架。