An Autoinhibitory Mechanism for Nonsyntaxin SNARE Proteins Revealed by the Structure of Ykt6p-Reference-Cited by-同舟云学术

An Autoinhibitory Mechanism for Nonsyntaxin SNARE Proteins Revealed by the Structure of Ykt6p

Published:2001-07-27 Issue:5530 Volume:293 Page:698-702
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Tochio Hidehito¹,Tsui Marco M. K.²,Banfield David K.²,Zhang Mingjie¹

Affiliation:

1. Department of Biochemistry and

2. Department of Biology, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China.

Abstract

Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH 2 -terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirely 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 NH 2 -terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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