4m66
From Proteopedia
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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=4m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m66 RCSB], [http://www.ebi.ac.uk/pdbsum/4m66 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=4m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m66 RCSB], [http://www.ebi.ac.uk/pdbsum/4m66 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RIPK3_MOUSE RIPK3_MOUSE]] Essential for programmed necrosis in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (By similarity).<ref>PMID:19590578</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 16:01, 25 December 2014
Crystal structure of the mouse RIP3 kinase domain
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