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

Journal Article · Sat Apr 01 04:00:00 EST 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106010062· OSTI ID:22356351

Kitano, Ken; Yusa, Fumie ^[1]; Hakoshima, Toshio ^[1]

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1. Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192 (Japan)

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.

• OSTI ID: 22356351
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ADHESION
CRYSTAL STRUCTURE
MASKING
MEMBRANES
MOLECULES
PROTEINS