7AJL

Cyrstal structure of CYRI-B/Fam49B

これはPDB形式変換不可エントリーです。

7AJL の概要

• エントリーDOI: 10.2210/pdb7ajl/pdb
• 分子名称: CYFIP-related Rac1 interactor B (2 entities in total)
• 機能のキーワード: rac1 competitor, actin regulation, scar/wave inhibitor, cytosolic protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68799.49

構造登録者

Yelland, T.,Anh, H.,Insall, R.,Machesky, L.,Ismail, S. (登録日: 2020-09-29, 公開日: 2020-11-18, 最終更新日: 2024-10-16)

主引用文献

Yelland, T.,Le, A.H.,Nikolaou, S.,Insall, R.,Machesky, L.,Ismail, S.
Structural Basis of CYRI-B Direct Competition with Scar/WAVE Complex for Rac1.
Structure, 29:226-237.e4, 2021

PubMed Abstract: Rac1 is a major regulator of actin dynamics, with GTP-bound Rac1 promoting actin assembly via the Scar/WAVE complex. CYRI competes with Scar/WAVE for interaction with Rac1 in a feedback loop regulating actin dynamics. Here, we reveal the nature of the CYRI-Rac1 interaction, through crystal structures of CYRI-B lacking the N-terminal helix (CYRI-BΔN) and the CYRI-BΔN:Rac1Q61L complex, providing the molecular basis for CYRI-B regulation of the Scar/WAVE complex. We reveal CYRI-B as having two subdomains - an N-terminal Rac1 binding subdomain with a unique Rac1-effector interface and a C-terminal Ratchet subdomain that undergoes conformational changes induced by Rac1 binding. Finally, we show that the CYRI protein family, CYRI-A and CYRI-B can produce an autoinhibited hetero- or homodimers, adding an additional layer of regulation to Rac1 signaling.

PubMed: 33217330
DOI: 10.1016/j.str.2020.11.003

実験手法

X-RAY DIFFRACTION (2.37 Å)