5VNY

Crystal structure of DM14-3 domain of Lgd

5VNY の概要

• エントリーDOI: 10.2210/pdb5vny/pdb
• 分子名称: Lethal (2) giant discs 1, isoform B (2 entities in total)
• 機能のキーワード: escrt, endocytosis, protein binding
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7426.28

構造登録者

McMillan, B.J.,Blacklow, S.C. (登録日: 2017-05-01, 公開日: 2017-06-14, 最終更新日: 2024-11-20)

主引用文献

McMillan, B.J.,Tibbe, C.,Drabek, A.A.,Seegar, T.C.M.,Blacklow, S.C.,Klein, T.
Structural Basis for Regulation of ESCRT-III Complexes by Lgd.
Cell Rep, 19:1750-1757, 2017

PubMed Abstract: The ESCRT-III complex induces outward membrane budding and fission through homotypic polymerization of its core component Shrub/CHMP4B. Shrub activity is regulated by its direct interaction with a protein called Lgd in flies, or CC2D1A or B in humans. Here, we report the structural basis for this interaction and propose a mechanism for regulation of polymer assembly. The isolated third DM14 repeat of Lgd binds Shrub, and an Lgd fragment containing only this DM14 repeat and its C-terminal C2 domain is sufficient for in vivo function. The DM14 domain forms a helical hairpin with a conserved, positively charged tip, that, in the structure of a DM14 domain-Shrub complex, occupies a negatively charged surface of Shrub that is otherwise used for homopolymerization. Lgd mutations at this interface disrupt its function in flies, confirming functional importance. Together, these data argue that Lgd regulates ESCRT activity by controlling access to the Shrub self-assembly surface.

PubMed: 28564595
DOI: 10.1016/j.celrep.2017.05.026

実験手法

X-RAY DIFFRACTION (1.101 Å)