PDBsum entry 5efx

Signaling protein

PDB id: 5efx

Contents

Protein chain

144 a.a.

Waters ×30

PDB id:

5efx

Name:

Signaling protein

Title:

Crystal structure of rho gtpase regulator

Structure:

Rho guanine nucleotide exchange factor 2. Chain: a. Fragment: unp residues 439-582. Synonym: guanine nucleotide exchange factor h1,gef-h1,microtubule- regulated rho-gef,proliferating cell nucleolar antigen p40. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: arhgef2, kiaa0651, lfp40. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768

Resolution:

2.45Å R-factor: 0.219 R-free: 0.253

Authors:

Y.Jiang,S.Ouyang,Z.J.Liu

Key ref:

Y.Jiang et al. (2016). Crystal structure of hGEF-H1 PH domain provides insight into incapability in phosphoinositide binding. Biochem Biophys Res Commun, 471, 621-627. PubMed id: 26820534 DOI: 10.1016/j.bbrc.2016.01.150

Date:

26-Oct-15 Release date: 29-Jun-16

Protein chain

Q92974  (ARHG2_HUMAN) -  Rho guanine nucleotide exchange factor 2 from Homo sapiens

Seq: 986 a.a.

Struc: 144 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.bbrc.2016.01.150

Biochem Biophys Res Commun 471:621-627 (2016)

PubMed id: 26820534

Crystal structure of hGEF-H1 PH domain provides insight into incapability in phosphoinositide binding.

Y.Jiang, H.Jiang, S.Zhou, B.Meng, Z.J.Liu, S.Ouyang.

ABSTRACT

The guanine nucleotide exchange factor GEF-H1 (also known as ARHGEF2) is identified as a member of the Dbl family of GEFs. It regulates RhoA-dependent cell signaling pathways and plays important roles in biological processes. GEF-H1 contains an N-terminal zinc finger domain, a Dbl-homologous (DH) domain followed by a Pleckstrin homology (PH) domain, and a C-terminal domain. The specific roles of its PH domain are poorly understood. Here we report the crystal structure of human GEF-H1 PH domain to 2.45 Å resolution. A conserved surface is formed by β8, β9, β10, and it may mediate protein-protein interactions. Although the folding resembles other PH domains that have defined structures, superposition of different PH domains clearly shows that the loop between β6/β7 and the loop between β3/β4 are so close that they will prevent its binding with phosphoinositide due to steric hindrance, and this has been proved by isothermal titration calorimetry (ITC) and thermal shift assay (TSA). Our studies provide a structural framework for further work on the function of GEF-H1.