Piecing together the ESCRTs

被引:11
|
作者
Hurley, James H. [1 ]
Im, Young Jun [1 ]
Lee, Hyung Ho [1 ]
Ren, Xuefeng [1 ]
Wollert, Thomas [1 ]
Yang, Dong [1 ]
机构
[1] NIDDK, Mol Biol Lab, NIH, US Dept HHS, Bethesda, MD 20892 USA
关键词
ALG-2 (apoptosis-linked gene 2)-interacting protein X (Alix); endosomal sorting complex required for transport (ESCRT); membrane; small-angle X-ray scattering (SAXS); ubiquitin; C-TERMINAL DOMAIN; STRUCTURAL BASIS; UBIQUITIN RECOGNITION; TRAFFICKING COMPLEX; EAP45-GLUE DOMAIN; CRYSTAL-STRUCTURE; GLUE DOMAIN; PROTEIN; VPS4; PATHWAY;
D O I
10.1042/BST0370161
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
High-resolution structural analysis has characterized nearly all of the individual domains of ESCRT (endosomal sorting complex required for transport) subunits, all of the core structures of the soluble complexes and many of the interactions involving domains. Recent emphasis in structural studies has shifted towards efforts to integrate these structures into a larger-scale model. molecular simulations, hydrodynamic analysis, small-angle X-ray scattering and cryo-EM (electron microscopy) techniques have all been brought to bear on the ESCRT system over the last year.
引用
收藏
页码:161 / 166
页数:6
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