2d2q

Publication Abstract from PubMed

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.

Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.,Kitano K, Yusa F, Hakoshima T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:16582480^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.