1ef1
From Proteopedia
(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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| - | [[Image:1ef1.gif|left|200px]]<br /> | + | [[Image:1ef1.gif|left|200px]]<br /><applet load="1ef1" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ef1" size=" | + | |
caption="1ef1, resolution 1.9Å" /> | caption="1ef1, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell | + | 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== | ==About this Structure== | ||
| - | 1EF1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EF1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EF1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bretscher, A.]] | [[Category: Bretscher, A.]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
| - | [[Category: Pearson, M | + | [[Category: Pearson, M A.]] |
[[Category: Reczek, D.]] | [[Category: Reczek, D.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: tail domain]] | [[Category: tail domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:05 2008'' |
Revision as of 10:27, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 12:27:05 2008
