An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p |
| |
| Authors: | Tochio H Tsui M M Banfield D K Zhang M |
| |
| Affiliation: | Department of Biochemistry, 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 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. |
| |
| Keywords: | |
| 本文献已被 PubMed 等数据库收录！ |
|
