| First Author | Kitano K | Year | 2006 |
| Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun | Volume | 62 |
| Issue | Pt 4 | Pages | 340-5 |
| PubMed ID | 16582480 | Mgi Jnum | J:222683 |
| Mgi Id | MGI:5645209 | Doi | 10.1107/S1744309106010062 |
| Citation | Kitano K, et al. (2006) Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304. Acta Crystallogr Sect F Struct Biol Cryst Commun 62(Pt 4):340-5 |
| abstractText | 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. |
