Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295–304
Acta Crystallographica Section F
Volume 62, Issue 4, pages 340–345, April 2006
How to Cite
Yusa, F., Kitano, K. and Hakoshima, T. (2006), Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295–304. Acta Crystallographica Section F, 62: 340–345. doi: 10.1107/S1744309106010062
- FERM domain;
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.