2d2q: Difference between revisions

[[Image:2d2q.gif|left|200px]]<br /><applet load="2d2q" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

2D2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2Q OCA].  

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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16582480 16582480]

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