Ontology highlight
ABSTRACT:
SUBMITTER: Wang S
PROVIDER: S-EPMC5350566 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Wang Shen S Choi Ucheor B UB Gong Jihong J Yang Xiaoyu X Li Yun Y Wang Austin L AL Yang Xiaofei X Brunger Axel T AT Ma Cong C
The EMBO journal 20170130 6
The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein syntaxin-1 adopts a closed conformation when bound to Munc18-1, preventing binding to synaptobrevin-2 and SNAP-25 to form the ternary SNARE complex. Although it is known that the MUN domain of Munc13-1 catalyzes the transition from the Munc18-1/syntaxin-1 complex to the SNARE complex, the molecular mechanism is unclear. Here, we identified two conserved residues (R151, I155) in the syntaxin-1 linker region ...[more]