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N-乙基马来酰亚胺敏感因子的六聚化结构域：伴侣功能的结构线索。

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

作者信息

Neuwald A F

机构信息

Cold Spring Harbor Laboratory, PO Box 1001, Bungtown Road, Cold Spring Harbor, NY 11724, USA.

出版信息

Structure. 1999 Feb 15;7(2):R19-23. doi: 10.1016/S0969-2126(99)80015-X.

DOI:10.1016/S0969-2126(99)80015-X
PMID:10368290
Abstract

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.

摘要

参与SNARE复合体拆解的分子伴侣N - 乙基马来酰亚胺敏感因子（NSF）的D2 ATP结合模块的六聚体结构最近已被确定。该结构以及先前确定的DNA聚合酶III δ'亚基的结构具有深远的生物学意义，因为这些模块与多种ATP酶相关，这些ATP酶促进各种蛋白质复合体的组装、拆解和运作。

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The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function.N-乙基马来酰亚胺敏感因子的六聚化结构域：伴侣功能的结构线索。
Structure. 1999 Feb 15;7(2):R19-23. doi: 10.1016/S0969-2126(99)80015-X.
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Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.N-乙基马来酰亚胺敏感融合蛋白六聚化结构域的晶体结构
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N-ethylmaleimide sensitive factor (NSF) structure and function.N-乙基马来酰亚胺敏感因子（NSF）的结构与功能。
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J Biol Chem. 1995 Dec 8;270(49):29182-8. doi: 10.1074/jbc.270.49.29182.

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