The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function

被引：21

作者：

Neuwald, AF ^{[1
]}

机构：

[1] Cold Spring Harbor Lab, Cold Spring Harbor, NY 11724 USA

来源：

STRUCTURE | 1999年 / 7卷 / 02期

关键词：

D O I：

10.1016/S0969-2126(99)80015-X

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：

The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-sensitive factor (NSF), a chaperone involved in SNARE complex disassembly, was recently determined. This structure and the previously determined structure of the DNA polymerase III delta' subunit have far-reaching biological significance because these modules are related to diverse ATPases that promote the assembly, disassembly and operation of various protein complexes.

引用

页码：R19 / R23

页数：5

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