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N-乙基马来酰亚胺敏感融合蛋白氨基末端结构域的晶体结构

Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein.

作者信息

May A P, Misura K M, Whiteheart S W, Weis W I

机构信息

Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.

出版信息

Nat Cell Biol. 1999 Jul;1(3):175-82. doi: 10.1038/11097.

Abstract

The cytosolic ATPase N-ethylmaleimide-sensitive fusion protein (NSF) disassembles complexes of membrane-bound proteins known as SNAREs, an activity essential for vesicular trafficking. The amino-terminal domain of NSF (NSF-N) is required for the interaction of NSF with the SNARE complex through the adaptor protein alpha-SNAP. The crystal structure of NSF-N reveals two subdomains linked by a single stretch of polypeptide. A polar interface between the two subdomains indicates that they can move with respect to one another during the catalytic cycle of NSF. Structure-based sequence alignments indicate that in addition to NSF orthologues, the p97 family of ATPases contain an amino-terminal domain of similar structure.

摘要

胞质ATP酶N - 乙基马来酰亚胺敏感融合蛋白(NSF)可拆解被称为SNAREs的膜结合蛋白复合物,这一活性对于囊泡运输至关重要。NSF的氨基末端结构域(NSF-N)通过衔接蛋白α-SNAP参与NSF与SNARE复合物的相互作用。NSF-N的晶体结构显示,两个亚结构域由一段多肽相连。两个亚结构域之间的极性界面表明,它们在NSF的催化循环中可相对移动。基于结构的序列比对表明,除了NSF直系同源物外,p97家族的ATP酶也含有结构相似的氨基末端结构域。

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