5UF7

CRYSTAL STRUCTURE OF MUNC13-1 MUN DOMAIN

5UF7 の概要

• エントリーDOI: 10.2210/pdb5uf7/pdb
• 関連するPDBエントリー: 5UE8
• 分子名称: Protein unc-13 homolog A (1 entity 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: 1
• 化学式量合計: 62849.93

構造登録者

Tomchick, D.R.,Rizo, J.,Xu, J. (登録日: 2017-01-03, 公開日: 2017-02-15, 最終更新日: 2023-10-04)

主引用文献

Xu, J.,Camacho, M.,Xu, Y.,Esser, V.,Liu, X.,Trimbuch, T.,Pan, Y.Z.,Ma, C.,Tomchick, D.R.,Rosenmund, C.,Rizo, J.
Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C1C2BMUN.
Elife, 6:-, 2017

PubMed Abstract: Munc13-1 acts as a master regulator of neurotransmitter release, mediating docking-priming of synaptic vesicles and diverse presynaptic plasticity processes. It is unclear how the functions of the multiple domains of Munc13-1 are coordinated. The crystal structure of a Munc13-1 fragment including its C, CB and MUN domains (CCBMUN) reveals a 19.5 nm-long multi-helical structure with the C and CB domains packed at one end. The similar orientations of the respective diacyglycerol- and Ca-binding sites of the C and CB domains suggest that the two domains cooperate in plasma-membrane binding and that activation of Munc13-1 by Ca and diacylglycerol during short-term presynaptic plasticity are closely interrelated. Electrophysiological experiments in mouse neurons support the functional importance of the domain interfaces observed in CCBMUN. The structure imposes key constraints for models of neurotransmitter release and suggests that Munc13-1 bridges the vesicle and plasma membranes from the periphery of the membrane-membrane interface.

PubMed: 28177287
DOI: 10.7554/eLife.22567

実験手法

X-RAY DIFFRACTION (2.896 Å)