1ef1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ef1 |SIZE=350|CAPTION= <scene name='initialview01'>1ef1</scene>, resolution 1.9Å | |PDB= 1ef1 |SIZE=350|CAPTION= <scene name='initialview01'>1ef1</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ef1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ef1 OCA], [http://www.ebi.ac.uk/pdbsum/1ef1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ef1 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Pearson, M A.]] | [[Category: Pearson, M A.]] | ||
[[Category: Reczek, D.]] | [[Category: Reczek, D.]] | ||
| - | [[Category: SO4]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: ferm domain]] | [[Category: ferm domain]] | ||
| Line 32: | Line 34: | ||
[[Category: tail domain]] | [[Category: tail domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:19 2008'' |
Revision as of 17:01, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 20:01:19 2008
