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==Cryo-EM structure of amyloid fibril formed by human RIPK3==
==Cryo-EM structure of amyloid fibril formed by human RIPK3==
<StructureSection load='7da4' size='340' side='right'caption='[[7da4]]' scene=''>
<StructureSection load='7da4' size='340' side='right'caption='[[7da4]], [[Resolution|resolution]] 4.24&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DA4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7da4]] is a 3 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=7DA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DA4 FirstGlance]. <br>
</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=7da4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7da4 OCA], [https://pdbe.org/7da4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7da4 RCSB], [https://www.ebi.ac.uk/pdbsum/7da4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7da4 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.24&#8491;</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=7da4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7da4 OCA], [https://pdbe.org/7da4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7da4 RCSB], [https://www.ebi.ac.uk/pdbsum/7da4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7da4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RIPK3_HUMAN RIPK3_HUMAN] Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL 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.<ref>PMID:19498109</ref> <ref>PMID:19524512</ref> <ref>PMID:19524513</ref> <ref>PMID:22265413</ref> <ref>PMID:22265414</ref> <ref>PMID:22421439</ref>
==See Also==
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Li D]]
[[Category: Li D]]

Latest revision as of 13:53, 27 March 2024

Cryo-EM structure of amyloid fibril formed by human RIPK3Cryo-EM structure of amyloid fibril formed by human RIPK3

Structural highlights

7da4 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 4.24Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RIPK3_HUMAN Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL 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.[1] [2] [3] [4] [5] [6]

See Also

References

  1. ↑ Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC, Dong MQ, Han J. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science. 2009 Jul 17;325(5938):332-6. doi: 10.1126/science.1172308. Epub 2009 Jun, 4. PMID:19498109 doi:http://dx.doi.org/10.1126/science.1172308
  2. ↑ He S, Wang L, Miao L, Wang T, Du F, Zhao L, Wang X. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell. 2009 Jun 12;137(6):1100-11. doi: 10.1016/j.cell.2009.05.021. PMID:19524512 doi:10.1016/j.cell.2009.05.021
  3. ↑ Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M, Chan FK. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell. 2009 Jun 12;137(6):1112-23. doi: 10.1016/j.cell.2009.05.037. PMID:19524513 doi:10.1016/j.cell.2009.05.037
  4. ↑ Sun L, Wang H, Wang Z, He S, Chen S, Liao D, Wang L, Yan J, Liu W, Lei X, Wang X. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell. 2012 Jan 20;148(1-2):213-27. doi: 10.1016/j.cell.2011.11.031. PMID:22265413 doi:http://dx.doi.org/10.1016/j.cell.2011.11.031
  5. ↑ Wang Z, Jiang H, Chen S, Du F, Wang X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell. 2012 Jan 20;148(1-2):228-43. doi: 10.1016/j.cell.2011.11.030. PMID:22265414 doi:http://dx.doi.org/10.1016/j.cell.2011.11.030
  6. ↑ Zhao J, Jitkaew S, Cai Z, Choksi S, Li Q, Luo J, Liu ZG. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):5322-7. doi:, 10.1073/pnas.1200012109. Epub 2012 Mar 15. PMID:22421439 doi:http://dx.doi.org/10.1073/pnas.1200012109

7da4, resolution 4.24Å

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