1ef1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:24, 6 November 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1ef1.png|left|200px]]
 
-
<!--
+
==CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX==
-
The line below this paragraph, containing "STRUCTURE_1ef1", creates the "Structure Box" on the page.
+
<StructureSection load='1ef1' size='340' side='right'caption='[[1ef1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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>
-
{{STRUCTURE_1ef1| PDB=1ef1 | SCENE= }}
+
<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.
-
===CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX===
+
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>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1ef1" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_10847681}}, adds the Publication Abstract to the page
+
*[[Moesin|Moesin]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 10847681 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_10847681}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
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].
+
-
 
+
-
==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:[http://www.ncbi.nlm.nih.gov/pubmed/10847681 10847681]
+
[[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 Tue Jul 1 00:35:54 2008''
+

Current revision

CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

PDB ID 1ef1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools