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Science 27 July 2001:
Vol. 293. no. 5530, pp. 698 - 702
DOI: 10.1126/science.1062950
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Reports

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

Hidehito Tochio,1* Marco M. K. Tsui,2* David K. Banfield,2dagger Mingjie Zhang1dagger

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 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 NH2-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.

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.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: bodkb{at}ust.hk, mzhang{at}ust.hk

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