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[[Image:1ef1.gif|left|200px]]
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{{STRUCTURE_1ef1|  PDB=1ef1  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX'''


==CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX==
<StructureSection load='1ef1' size='340' side='right'caption='[[1ef1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ef1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EF1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ef1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ef1 OCA], [https://pdbe.org/1ef1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ef1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ef1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ef1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOES_HUMAN MOES_HUMAN] Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage.<ref>PMID:21549406</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/1ef1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ef1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:10847681</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1EF1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EF1 OCA].
</div>
<div class="pdbe-citations 1ef1" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10847681 10847681]
*[[Moesin|Moesin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bretscher, A.]]
[[Category: Bretscher A]]
[[Category: Karplus, P A.]]
[[Category: Karplus PA]]
[[Category: Pearson, M A.]]
[[Category: Pearson MA]]
[[Category: Reczek, D.]]
[[Category: Reczek D]]
[[Category: Crystal structure]]
[[Category: Ferm domain]]
[[Category: Membrane]]
[[Category: Tail domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:01:02 2008''

Latest revision as of 08:24, 6 November 2024

CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

1ef1, resolution 1.90Å

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