1ef1

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[[Image:1ef1.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1ef1| PDB=1ef1 | SCENE= }}
{{STRUCTURE_1ef1| PDB=1ef1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX'''
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===CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10847681 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10847681}}
==About this Structure==
==About this Structure==
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[[Category: Membrane]]
[[Category: Membrane]]
[[Category: Tail domain]]
[[Category: Tail domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:01:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:35:54 2008''

Revision as of 21:35, 30 June 2008

Image:1ef1.png

Template:STRUCTURE 1ef1

CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

Template:ABSTRACT PUBMED 10847681

About this Structure

1EF1 is a Protein complex structure of sequences from Homo sapiens. 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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