2efk: Difference between revisions

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<StructureSection load='2efk' size='340' side='right'caption='[[2efk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2efk' size='340' side='right'caption='[[2efk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2efk]] is a 1 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=2EFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFK FirstGlance]. <br>
<table><tr><td colspan='2'>[[2efk]] is a 1 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=2EFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFK FirstGlance]. <br>
</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>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=2efk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efk OCA], [https://pdbe.org/2efk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efk RCSB], [https://www.ebi.ac.uk/pdbsum/2efk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efk ProSAT], [https://www.topsan.org/Proteins/RSGI/2efk TOPSAN]</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=2efk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efk OCA], [https://pdbe.org/2efk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efk RCSB], [https://www.ebi.ac.uk/pdbsum/2efk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efk ProSAT], [https://www.topsan.org/Proteins/RSGI/2efk TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CIP4_HUMAN CIP4_HUMAN]] Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:11069762</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref>
[https://www.uniprot.org/uniprot/CIP4_HUMAN CIP4_HUMAN] Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:11069762</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/2efk_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/2efk_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, L]]
[[Category: Chen L]]
[[Category: Liu, Z J]]
[[Category: Liu Z-J]]
[[Category: Niwa, H]]
[[Category: Niwa H]]
[[Category: Structural genomic]]
[[Category: Shimada A]]
[[Category: Shimada, A]]
[[Category: Shirouzu M]]
[[Category: Shirouzu, M]]
[[Category: Terada T]]
[[Category: Terada, T]]
[[Category: Wang B-C]]
[[Category: Wang, B C]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S]]
[[Category: Efc domain]]
[[Category: Endocytosis-exocytosis complex]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Rsgi]]

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