PDBsum entry 2d2q

Cell adhesion

PDB id: 2d2q

Contents

Protein chains

297 a.a. *

* Residue conservation analysis

PDB id:

2d2q

Name:

Cell adhesion

Title:

Crystal structure of the dimerized radixin ferm domain

Structure:

Radixin. Chain: a, b. Fragment: ferm domain (residues 1-310). Synonym: esp10. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.80Å R-factor: 0.222 R-free: 0.269

Authors:

K.Kitano,F.Yusa,T.Hakoshima

Key ref:

K.Kitano et al. (2006). Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 340-345. PubMed id: 16582480 DOI: 10.1107/S1744309106010062

Date:

15-Sep-05 Release date: 18-Apr-06

Protein chains

P26043  (RADI_MOUSE) -  Radixin from Mus musculus

Seq: 583 a.a.

Struc: 297 a.a.

DOI no: 10.1107/S1744309106010062

Acta Crystallograph Sect F Struct Biol Cryst Commun 62:340-345 (2006)

PubMed id: 16582480

Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.

K.Kitano, F.Yusa, T.Hakoshima.

ABSTRACT

ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion molecules in the formation of the membrane-associated cytoskeleton. The binding site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the inactive form. A conventional masking motif, strand 1 (residues 494-500 in radixin), has previously been identified in the C-terminal tail domain. Here, the crystal structure of dimerized radixin FERM domains (residues 1-310) is presented in which the binding site of one molecule is occupied by the C-terminal residues (residues 295-304, strand 2) of the other molecule. The residues contain a conserved motif that is compatible with that identified in the adhesion molecules. The residues might serve as a second masking region in the inactive form of ERM proteins.

Selected figure(s)

Figure 1.
Figure 1 Crystal structure of dimerized radixin FERM domains. (a) Overall structure as a ribbon model. Mol-1 is shown in light blue and Mol-2 in pink, with its C-terminal extended residues (Arg295-Gln304) in red. The radixin FERM domain consists of subdomains A (the N-terminal 82 residues), B (residues 96-119) and C (residues 204-297). (b) A side view shows that Mol-1 and Mol-2 are aligned in a similar orientation. The blue dashed line represents the membrane-interaction surface of a dimer and blue arrows indicate binding sites to phosphatidylinositol 4,5-bisphosphate (PIP2; Hamada, Shimizu et al., 2000[Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. & Hakoshima, T. (2000). EMBO J. 19, 4449-4462.]). Figures were prepared using PyMOL (http://pymol.sourceforge.net ). (c) Schematic representation of the interactions between the C-terminal extended residues (strand 2 in pink) and subdomain C (light blue). Hydrogen bonds are shown as dashed lines and distances are indicated.

The above figure is reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 340-345) copyright 2006.

Figure was selected by an automated process.