Open AccessStructure of dimerized radixin FERM domain suggests a novel masking motif in C‐terminal residues 295–304
Author(s) -
Yusa Fumie,
Kitano Ken,
Hakoshima Toshio
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106010062
Subject(s) - radixin , moesin , ezrin , chemistry , biophysics , ferm domain , molecule , cytoplasm , binding site , microbiology and biotechnology , crystallography , cytoskeleton , biochemistry , membrane protein , biology , membrane , integral membrane protein , organic chemistry , cell
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.