7D2G

Coiled-coil structure of liprin-alpha2_H2delC

7D2G の概要

• エントリーDOI: 10.2210/pdb7d2g/pdb
• 分子名称: Liprin-alpha-2, GLYCEROL (3 entities in total)
• 機能のキーワード: coiled-coil, protein binding
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 25904.38

構造登録者

Liang, M.,Wei, Z. (登録日: 2020-09-16, 公開日: 2021-04-07)

主引用文献

Liang, M.,Jin, G.,Xie, X.,Zhang, W.,Li, K.,Niu, F.,Yu, C.,Wei, Z.
Oligomerized liprin-alpha promotes phase separation of ELKS for compartmentalization of presynaptic active zone proteins.
Cell Rep, 34:108901-108901, 2021

PubMed Abstract: Synaptic scaffold proteins (e.g., liprin-α, ELKS, RIM, and RIM-BP) orchestrate ion channels, receptors, and enzymes at presynaptic terminals to form active zones for neurotransmitter release. The underlying mechanism of the active zone assembly remains elusive. Here, we report that liprin-α proteins have the potential to oligomerize through the N-terminal coiled-coil region. Our structural and biochemical characterizations reveal that a gain-of-function mutation promotes the self-assembly of the coiled coils in liprin-α2 by disrupting intramolecular interactions and promoting intermolecular interactions. By enabling multivalent interactions with ELKS proteins, the oligomerized coiled-coil region of liprin-α2 enhances the phase separation of the ELKS N-terminal segment. We further show that liprin-α2, by regulating the interplay between two phase separations of ELKS and RIM/RIM-BP, controls the protein distributions. These results imply that the complicated protein-protein interactions allow liprin-α to function with the active zone scaffolds and compartmentalize protein assemblies to achieve comprehensive functions in the active zone.

PubMed: 33761347
DOI: 10.1016/j.celrep.2021.108901

実験手法

X-RAY DIFFRACTION (1.7 Å)