7m4o

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of phosphorylated RBR E3 ligase RNF216 in complex with K63-linked di-ubiquitin

Structural highlights

7m4o 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:	X-ray diffraction, Resolution 2.21Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

RN216_HUMAN Cerebellar ataxia-hypogonadism syndrome. The disease is caused by variants affecting the gene represented in this entry.

Function

RN216_HUMAN E3 ubiquitin ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their ubiquitination (PubMed:34998453). Plays a role in the regulation of antiviral responses by promoting the degradation of TRAF3, TLR4 and TLR9 (PubMed:15107846, PubMed:19893624). In turn, down-regulates NF-kappa-B and IRF3 activation as well as beta interferon production. Participates also in the regulation of autophagy by ubiquitinating BECN1 leading to its degradation and autophagy inhibition (PubMed:25484083). Plays a role in ARC-dependent synaptic plasticity by mediating ARC ubiquitination resulting in its rapid proteasomal degradation (PubMed:24945773). Plays aso an essential role in spermatogenesis and male fertility (By similarity). Mechanistically, regulates meiosis by promoting the degradation of PRKACB through the ubiquitin-mediated lysosome pathway (By similarity). Modulates the gonadotropin-releasing hormone signal pathway by affecting the stability of STAU2 that is required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite (By similarity).[UniProtKB:P58283]^[1] ^[2] ^[3] ^[4] ^[5] Inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis.^[6]

References

↑ Chuang TH, Ulevitch RJ. Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors. Nat Immunol. 2004 May;5(5):495-502. doi: 10.1038/ni1066. Epub 2004 Apr 25. PMID:15107846 doi:http://dx.doi.org/10.1038/ni1066
↑ Nakhaei P, Mesplede T, Solis M, Sun Q, Zhao T, Yang L, Chuang TH, Ware CF, Lin R, Hiscott J. The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation. PLoS Pathog. 2009 Nov;5(11):e1000650. doi: 10.1371/journal.ppat.1000650. Epub , 2009 Nov 6. PMID:19893624 doi:http://dx.doi.org/10.1371/journal.ppat.1000650
↑ Mabb AM, Je HS, Wall MJ, Robinson CG, Larsen RS, Qiang Y, Corrêa SA, Ehlers MD. Triad3A regulates synaptic strength by ubiquitination of Arc. Neuron. 2014 Jun 18;82(6):1299-316. PMID:24945773 doi:10.1016/j.neuron.2014.05.016
↑ Xu C, Feng K, Zhao X, Huang S, Cheng Y, Qian L, Wang Y, Sun H, Jin M, Chuang TH, Zhang Y. Regulation of autophagy by E3 ubiquitin ligase RNF216 through BECN1 ubiquitination. Autophagy. 2014;10(12):2239-50. PMID:25484083 doi:10.4161/15548627.2014.981792
↑ Cotton TR, Cobbold SA, Bernardini JP, Richardson LW, Wang XS, Lechtenberg BC. Structural basis of K63-ubiquitin chain formation by the Gordon-Holmes syndrome RBR E3 ubiquitin ligase RNF216. Mol Cell. 2022 Feb 3;82(3):598-615.e8. PMID:34998453 doi:10.1016/j.molcel.2021.12.005
↑ Chen D, Li X, Zhai Z, Shu HB. A novel zinc finger protein interacts with receptor-interacting protein (RIP) and J Biol Chem. 2002 May 3;277(18):15985-91. PMID:11854271 doi:10.1074/jbc.M108675200

1 Structural highlights
2 Disease
3 Function
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7m4o"

Categories: Homo sapiens | Large Structures | Cotton TR | Lechtenberg BC

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7m4o is ON HOLD
+==Crystal structure of phosphorylated RBR E3 ligase RNF216 in complex with K63-linked di-ubiquitin==
+<StructureSection load='7m4o' size='340' side='right'caption='[[7m4o]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7m4o]] 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=7M4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M4O FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=7m4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m4o OCA], [https://pdbe.org/7m4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m4o RCSB], [https://www.ebi.ac.uk/pdbsum/7m4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m4o ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/RN216_HUMAN RN216_HUMAN] Cerebellar ataxia-hypogonadism syndrome. The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/RN216_HUMAN RN216_HUMAN] E3 ubiquitin ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their ubiquitination (PubMed:34998453). Plays a role in the regulation of antiviral responses by promoting the degradation of TRAF3, TLR4 and TLR9 (PubMed:15107846, PubMed:19893624). In turn, down-regulates NF-kappa-B and IRF3 activation as well as beta interferon production. Participates also in the regulation of autophagy by ubiquitinating BECN1 leading to its degradation and autophagy inhibition (PubMed:25484083). Plays a role in ARC-dependent synaptic plasticity by mediating ARC ubiquitination resulting in its rapid proteasomal degradation (PubMed:24945773). Plays aso an essential role in spermatogenesis and male fertility (By similarity). Mechanistically, regulates meiosis by promoting the degradation of PRKACB through the ubiquitin-mediated lysosome pathway (By similarity). Modulates the gonadotropin-releasing hormone signal pathway by affecting the stability of STAU2 that is required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite (By similarity).[UniProtKB:P58283]<ref>PMID:15107846</ref> <ref>PMID:19893624</ref> <ref>PMID:24945773</ref> <ref>PMID:25484083</ref> <ref>PMID:34998453</ref>   Inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis.<ref>PMID:11854271</ref>
-Authors:
+==See Also==
+*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
-Description:
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
-[[Category: Unreleased Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Cotton TR]]
+[[Category: Lechtenberg BC]]

7m4o

From Proteopedia

Current revision

Crystal structure of phosphorylated RBR E3 ligase RNF216 in complex with K63-linked di-ubiquitin

Structural highlights

Disease

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox