3SWH

Munc13-1, MUN domain, C-terminal module

3SWH の概要

• エントリーDOI: 10.2210/pdb3swh/pdb
• 分子名称: Protein unc-13 homolog A (2 entities in total)
• 機能のキーワード: alpha helical, neurotransmitter release, snare motif, exocytosis
• 由来する生物種: Rattus norvegicus (rat); 詳細
• 細胞内の位置: Cytoplasm: Q62768
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77473.04

構造登録者

Tomchick, D.R.,Rizo, J.,Li, W. (登録日: 2011-07-13, 公開日: 2011-11-02, 最終更新日: 2024-02-28)

主引用文献

Li, W.,Ma, C.,Guan, R.,Xu, Y.,Tomchick, D.R.,Rizo, J.
The Crystal Structure of a Munc13 C-terminal Module Exhibits a Remarkable Similarity to Vesicle Tethering Factors.
Structure, 19:1443-1455, 2011

PubMed Abstract: Unc13/Munc13s play a crucial function in neurotransmitter release through their MUN domain, which mediates the transition from the Syntaxin-1/Munc18-1 complex to the SNARE complex. The MUN domain was suggested to be related to tethering factors, but no MUN-domain structure is available to experimentally validate this notion and address key unresolved questions about the interactions and minimal structural unit required for Unc13/Munc13 function. Here we identify an autonomously folded module within the MUN domain (MUN-CD) and show that its crystal structure is remarkably similar to several tethering factors. We also show that the activity in promoting the Syntaxin-1/Munc18-1 to SNARE complex transition is strongly impaired in MUN-CD. These results show that MUN domains and tethering factors indeed belong to the same family and may have a common role in membrane trafficking. We propose a model whereby the MUN-CD module is central for Munc13 function but full activity requires adjacent sequences.

PubMed: 22000513
DOI: 10.1016/j.str.2011.07.012

実験手法

X-RAY DIFFRACTION (2.65 Å)