7KDC

The complex between RhoD and the Plexin B2 RBD

7KDC の概要

• エントリーDOI: 10.2210/pdb7kdc/pdb
• 分子名称: Rho-related GTP-binding protein RhoD, Plexin-B2, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: plexin, rhod, gtpase, axon guidance, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67147.26

構造登録者

Kuo, Y.,Wang, Y.,Zhang, x. (登録日: 2020-10-08, 公開日: 2021-07-28, 最終更新日: 2024-11-20)

主引用文献

Liu, Y.,Ke, P.,Kuo, Y.C.,Wang, Y.,Zhang, X.,Song, C.,Shan, Y.
A putative structural mechanism underlying the antithetic effect of homologous RND1 and RhoD GTPases in mammalian plexin regulation.
Elife, 10:-, 2021

PubMed Abstract: Plexins are semaphorin receptors that play essential roles in mammalian neuronal axon guidance and in many other important mammalian biological processes. Plexin signaling depends on a semaphorin-induced dimerization mechanism and is modulated by small GTPases of the Rho family, of which RND1 serves as a plexin activator yet its close homolog RhoD an inhibitor. Using molecular dynamics (MD) simulations, we showed that RND1 reinforces the plexin dimerization interface, whereas RhoD destabilizes it due to their differential interaction with the cell membrane. Upon binding plexin at the Rho-GTPase-binding domain (RBD), RND1 and RhoD interact differently with the inner leaflet of the cell membrane and exert opposite effects on the dimerization interface via an allosteric network involving the RBD, RBD linkers, and a buttress segment adjacent to the dimerization interface. The differential membrane interaction is attributed to the fact that, unlike RND1, RhoD features a short C-terminal tail and a positively charged membrane interface.

PubMed: 34114565
DOI: 10.7554/eLife.64304

実験手法

X-RAY DIFFRACTION (3.1 Å)