2l6l
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2l6l]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L6L FirstGlance]. <br> | <table><tr><td colspan='2'>[[2l6l]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L6L FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </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> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l6l RCSB], [http://www.ebi.ac.uk/pdbsum/2l6l PDBsum]</span></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=2l6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l6l RCSB], [http://www.ebi.ac.uk/pdbsum/2l6l PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Atreya, H S | + | [[Category: Atreya, H S]] |
| - | [[Category: Chitoor, B S | + | [[Category: Chitoor, B S]] |
| - | [[Category: Silva, P D | + | [[Category: Silva, P D]] |
| - | [[Category: Thakur, A | + | [[Category: Thakur, A]] |
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Dph4]] | [[Category: Dph4]] | ||
[[Category: J-domain]] | [[Category: J-domain]] | ||
[[Category: Zn-csl]] | [[Category: Zn-csl]] | ||
Revision as of 13:31, 25 December 2014
Solution structure of human J-protein co-chaperone, Dph4
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Categories: Homo sapiens | Atreya, H S | Chitoor, B S | Silva, P D | Thakur, A | Chaperone | Dph4 | J-domain | Zn-csl
