1ef1
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(New page: 200px<br /> <applet load="1ef1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ef1, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:36, 12 November 2007
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CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX
Overview
The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell, surface structures to the plasma membrane, using a C-terminal F-actin, binding segment and an N-terminal FERM domain, a common membrane binding, module. ERM proteins are regulated by an intramolecular association of the, FERM and C-terminal tail domains that masks their binding sites. The, crystal structure of a dormant moesin FERM/tail complex reveals that the, FERM domain has three compact lobes including an integrated PTB/PH/ EVH1, fold, with the C-terminal segment bound as an extended peptide masking a, large surface of the FERM domain. This extended binding mode suggests a, novel mechanism for how different signals could produce varying levels of, activation. Sequence conservation suggests a similar regulation of the, tumor suppressor merlin.
About this Structure
1EF1 is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain., Pearson MA, Reczek D, Bretscher A, Karplus PA, Cell. 2000 Apr 28;101(3):259-70. PMID:10847681
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