2d2q
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="2d2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d2q, resolution 2.8Å" /> '''Crystal structure of ...)
Next diff →
Revision as of 07:17, 21 November 2007
|
Crystal structure of the dimerized radixin FERM domain
Overview
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.
About this Structure
2D2Q is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304., Kitano K, Yusa F, Hakoshima T, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:16582480
Page seeded by OCA on Wed Nov 21 09:24:25 2007
