An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p

被引：113

作者：

Tochio, H

Tsui, MMK

Banfield, DK

Zhang, MJ

机构：

[1] Hong Kong Univ Sci & Technol, Dept Biochem, Kowloon, Hong Kong, Peoples R China

[2] Hong Kong Univ Sci & Technol, Dept Biol, Kowloon, Hong Kong, Peoples R China

来源：

SCIENCE | 2001年 / 293卷 / 5530期

关键词：

D O I：

10.1126/science.1062950

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirety from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin. Like some syntaxins, Ykt6p adopted a folded back conformation in which Ykt6pN bound to its COOH-terminal core domain. The NH2-terminal domain plays an important biological rote in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes.

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页码：698 / 702

页数：5

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