2d2q

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|ACTIVITY=
|ACTIVITY=
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|RELATEDENTRY=[[1gc7|1GC7]], [[1gc6|1GC6]], [[1j19|1J19]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2q OCA], [http://www.ebi.ac.uk/pdbsum/2d2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d2q RCSB]</span>
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[[Category: masking]]
[[Category: masking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:34 2008''

Revision as of 23:29, 30 March 2008


PDB ID 2d2q

Drag the structure with the mouse to rotate
, resolution 2.8Å
Related: 1GC7, 1GC6, 1J19


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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