PDBsum entry 6d2k

Signaling protein

PDB id: 6d2k

Contents

Protein chain

286 a.a.

Waters ×290

PDB id:

6d2k

Name:

Signaling protein

Title:

Crystal structure of the ferm domain of mouse farp2

Structure:

Ferm, arhgef and pleckstrin domain-containing protein 2. Chain: a. Synonym: ferm domain including rhogef,fir,ferm,rhogef and pleckstrin domain-containing protein 2. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: farp2, kiaa0793. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.55Å R-factor: 0.198 R-free: 0.224

Authors:

X.He,X.Zhang

Key ref:

Y.C.Kuo et al. (2018). Structural analyses of FERM domain-mediated membrane localization of FARP1. Sci Rep, 8, 10477. PubMed id: 29992992

Date:

13-Apr-18 Release date: 18-Jul-18

Protein chain

Q91VS8  (FARP2_MOUSE) -  FERM, ARHGEF and pleckstrin domain-containing protein 2 from Mus musculus

Seq: 1065 a.a.

Struc: 286 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Sci Rep 8:10477 (2018)

PubMed id: 29992992

Structural analyses of FERM domain-mediated membrane localization of FARP1.

Y.C.Kuo, X.He, A.J.Coleman, Y.J.Chen, P.Dasari, J.Liou, T.Biederer, X.Zhang.

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.