6D2Q

Crystal structure of the FERM domain of zebrafish FARP1

6D2Q の概要

• エントリーDOI: 10.2210/pdb6d2q/pdb
• 関連するPDBエントリー: 6D21
• 分子名称: FERM, RhoGEF (ARHGEF) and pleckstrin domain protein 1 (chondrocyte-derived) (1 entity in total)
• 機能のキーワード: membrane targeting, signaling protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33361.81

構造登録者

Kuo, Y.C.,Zhang, X. (登録日: 2018-04-13, 公開日: 2018-07-18, 最終更新日: 2023-10-04)

主引用文献

Kuo, Y.C.,He, X.,Coleman, A.J.,Chen, Y.J.,Dasari, P.,Liou, J.,Biederer, T.,Zhang, X.
Structural analyses of FERM domain-mediated membrane localization of FARP1.
Sci Rep, 8:10477-10477, 2018

PubMed Abstract: FARP1 is a multi-domain protein that is involved in regulating neuronal development through interacting with cell surface proteins such as class A Plexins and SynCAM 1. The N-terminal FERM domain in FARP1 is known to both promote membrane localization and mediate these protein interactions, for which the underlying molecular mechanisms remain unclear. Here we determined the crystal structures of the FERM domain of FARP1 from zebrafish, and those of FARP2 (a close homolog of FARP1) from mouse and zebrafish. These FERM domains adopt the three-leaved clover fold that is typical of all FERM domains. Our structures reveal a positively charged surface patch that is highly conserved in the FERM domain of FARP1 and FARP2. In vitro lipid-binding experiments showed that the FARP1 FERM domain binds specifically to several types of phospholipid, which is dependent on the positively charged surface patch. We further determined through cell-based analyses that this surface patch on the FERM domain underlies the localization of FARP1 to the plasma membrane, and that FERM domain interactions recruit it to postsynaptic sites in neurons.

PubMed: 29992992
DOI: 10.1038/s41598-018-28692-4

実験手法

X-RAY DIFFRACTION (2.99 Å)