2vsz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:03, 9 May 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2vsz.png|left|200px]]
 
-
<!--
+
==Crystal Structure of the ELMO1 PH domain==
-
The line below this paragraph, containing "STRUCTURE_2vsz", creates the "Structure Box" on the page.
+
<StructureSection load='2vsz' size='340' side='right'caption='[[2vsz]], [[Resolution|resolution]] 2.30&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'>[[2vsz]] is a 2 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=2VSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VSZ 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]] 2.3&#8491;</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=2vsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsz OCA], [https://pdbe.org/2vsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vsz RCSB], [https://www.ebi.ac.uk/pdbsum/2vsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsz ProSAT]</span></td></tr>
-
{{STRUCTURE_2vsz| PDB=2vsz | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ELMO1_HUMAN ELMO1_HUMAN] Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.<ref>PMID:11595183</ref> <ref>PMID:12134158</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/vs/2vsz_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2vsz ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The mammalian DOCK180 protein belongs to an evolutionarily conserved protein family, which together with ELMO proteins, is essential for activation of Rac GTPase-dependent biological processes. Here, we have analyzed the DOCK180-ELMO1 interaction, and map direct interaction interfaces to the N-terminal 200 amino acids of DOCK180, and to the C-terminal 200 amino acids of ELMO1, comprising the ELMO1 PH domain. Structural and biochemical analysis of this PH domain reveals that it is incapable of phospholipid binding, but instead structurally resembles FERM domains. Moreover, the structure revealed an N-terminal amphiphatic alpha-helix, and point mutants of invariant hydrophobic residues in this helix disrupt ELMO1-DOCK180 complex formation. A secondary interaction between ELMO1 and DOCK180 is conferred by the DOCK180 SH3 domain and proline-rich motifs at the ELMO1 C-terminus. Mutation of both DOCK180-interaction sites on ELMO1 is required to disrupt the DOCK180-ELMO1 complex. Significantly, although this does not affect DOCK180 GEF activity toward Rac in vivo, Rac signaling is impaired, implying additional roles for ELMO in mediating intracellular Rac signaling.
-
===CRYSTAL STRUCTURE OF THE ELMO1 PH DOMAIN===
+
An alpha-helical extension of the ELMO1 pleckstrin homology domain mediates direct interaction to DOCK180 and is critical in Rac signaling.,Komander D, Patel M, Laurin M, Fradet N, Pelletier A, Barford D, Cote JF Mol Biol Cell. 2008 Nov;19(11):4837-51. Epub 2008 Sep 3. PMID:18768751<ref>PMID:18768751</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_18768751}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2vsz" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 18768751 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18768751}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2VSZ is a 2 chains structure with 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=2VSZ OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:18768751</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Barford, D.]]
+
[[Category: Large Structures]]
-
[[Category: Cote, J F.]]
+
[[Category: Barford D]]
-
[[Category: Komander, D.]]
+
[[Category: Cote J-F]]
-
[[Category: Patel, M.]]
+
[[Category: Komander D]]
-
[[Category: Apoptosis]]
+
[[Category: Patel M]]
-
[[Category: Dock180]]
+
-
[[Category: Elmo]]
+
-
[[Category: Guanine nucleotide exchange factor]]
+
-
[[Category: Phagocytosis]]
+
-
[[Category: Phosphoinositide binding]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Rac signalling]]
+
-
[[Category: Sh3-binding]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 09:13:53 2010''
+

Current revision

Crystal Structure of the ELMO1 PH domain

PDB ID 2vsz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vsz"
Personal tools