Structural highlights
Function
[RADI_MOUSE] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Kitano K, Yusa F, Hakoshima T. 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. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:16582480 doi:10.1107/S1744309106010062
