2d2q
From Proteopedia
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[[Image:2d2q.gif|left|200px]] | [[Image:2d2q.gif|left|200px]] | ||
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'''Crystal structure of the dimerized radixin FERM domain''' | '''Crystal structure of the dimerized radixin FERM domain''' | ||
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[[Category: Kitano, K.]] | [[Category: Kitano, K.]] | ||
[[Category: Yusa, F.]] | [[Category: Yusa, F.]] | ||
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- | [[Category: | + | [[Category: Masking]] |
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Revision as of 20:35, 3 May 2008
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 Crystallogr 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 Sat May 3 23:35:36 2008