3uiu

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<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=3uiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uiu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uiu RCSB], [http://www.ebi.ac.uk/pdbsum/3uiu 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=3uiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uiu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uiu RCSB], [http://www.ebi.ac.uk/pdbsum/3uiu PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/E2AK2_HUMAN E2AK2_HUMAN]] Following activation by double-stranded RNA in the presence of ATP, the kinase becomes autophosphorylated and can catalyze the phosphorylation of the translation initiation factor EIF2S1, which leads to an inhibition of the initiation of protein synthesis. Double-stranded RNA is generated during the course of a viral infection. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity: phosphorylates CDK1 upon DNA damage. CDK1 phosphorylation triggers CDK1 polyubiquitination and subsequent proteolysis, thus leading to G2 arrest.<ref>PMID:20395957</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 07:33, 25 December 2014

Crystal structure of Apo-PKR kinase domain

3uiu, resolution 2.90Å

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