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1ef1

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Revision as of 09:36, 21 July 2021

CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

Structural highlights

1ef1 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Henning MS, Stiedl P, Barry DS, McMahon R, Morham SG, Walsh D, Naghavi MH. PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1. Virology. 2011 Jul 5;415(2):114-21. doi: 10.1016/j.virol.2011.04.006. Epub 2011, May 6. PMID:21549406 doi:10.1016/j.virol.2011.04.006
↑ Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell. 2000 Apr 28;101(3):259-70. PMID:10847681

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ef1"

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EF1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ef1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ef1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ef1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ef1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ef1 ProSAT]</span></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 ==
-[[http://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>
+[[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]]
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 1ef1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Moesin|Moesin]]
 == References ==
 <references/>

1ef1

From Proteopedia

Revision as of 09:36, 21 July 2021

CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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