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2l6l
From Proteopedia
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==Solution structure of human J-protein co-chaperone, Dph4== | ==Solution structure of human J-protein co-chaperone, Dph4== | ||
| - | <StructureSection load='2l6l' size='340' side='right' caption='[[2l6l | + | <StructureSection load='2l6l' size='340' side='right'caption='[[2l6l]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2l6l]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2l6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2l6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6l OCA], [https://pdbe.org/2l6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6l RCSB], [https://www.ebi.ac.uk/pdbsum/2l6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DJC24_HUMAN DJC24_HUMAN] Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron-bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta).<ref>PMID:22509046</ref> <ref>PMID:22367199</ref> |
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| + | ==See Also== | ||
| + | *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Atreya HS]] |
| - | [[Category: | + | [[Category: Chitoor BS]] |
| - | [[Category: | + | [[Category: Silva PD]] |
| - | [[Category: | + | [[Category: Thakur A]] |
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Current revision
Solution structure of human J-protein co-chaperone, Dph4
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