skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

Abstract

The crystal structure of dimerized radixin FERM domain has been determined. It was found that the adhesion molecule-binding site of one molecule is masked by the C-terminal residues of the other molecule. 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.

Authors:
;  [1];  [1];  [2]
  1. Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192 (Japan)
  2. (Japan)
Publication Date:
OSTI Identifier:
22356351
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 4; Other Information: PMCID: PMC2222584; PMID: 16582480; PUBLISHER-ID: tb5004; OAI: oai:pubmedcentral.nih.gov:2222584; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ADHESION; CRYSTAL STRUCTURE; MASKING; MEMBRANES; MOLECULES; PROTEINS

Citation Formats

Kitano, Ken, Yusa, Fumie, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, and CREST, Japan Science and Technology Agency. Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295–304. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106010062.
Kitano, Ken, Yusa, Fumie, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, & CREST, Japan Science and Technology Agency. Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295–304. United Kingdom. doi:10.1107/S1744309106010062.
Kitano, Ken, Yusa, Fumie, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, and CREST, Japan Science and Technology Agency. Sat . "Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295–304". United Kingdom. doi:10.1107/S1744309106010062.
@article{osti_22356351,
title = {Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295–304},
author = {Kitano, Ken and Yusa, Fumie and Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp and CREST, Japan Science and Technology Agency},
abstractNote = {The crystal structure of dimerized radixin FERM domain has been determined. It was found that the adhesion molecule-binding site of one molecule is masked by the C-terminal residues of the other molecule. 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.},
doi = {10.1107/S1744309106010062},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 62,
place = {United Kingdom},
year = {Sat Apr 01 00:00:00 EST 2006},
month = {Sat Apr 01 00:00:00 EST 2006}
}