8f2r: Difference between revisions

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New page: '''Unreleased structure''' The entry 8f2r is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 8f2r is ON HOLD
==Human CCC complex==
 
<StructureSection load='8f2r' size='340' side='right'caption='[[8f2r]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8f2r]] is a 10 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=8F2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F2R FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.12&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f2r OCA], [https://pdbe.org/8f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f2r RCSB], [https://www.ebi.ac.uk/pdbsum/8f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f2r ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COMD1_HUMAN COMD1_HUMAN] Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.<ref>PMID:14685266</ref> <ref>PMID:15799966</ref> <ref>PMID:16573520</ref> <ref>PMID:17309234</ref> <ref>PMID:17183367</ref> <ref>PMID:20048074</ref> <ref>PMID:20595380</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Berger I]]
[[Category: Berger-Schaffitzel C]]
[[Category: Borucu U]]
[[Category: Butkovic R]]
[[Category: Caruana NJ]]
[[Category: Chen K]]
[[Category: Chilton M]]
[[Category: Collins BM]]
[[Category: Croll TI]]
[[Category: Cullen PJ]]
[[Category: Derivery E]]
[[Category: Ghai R]]
[[Category: Hall RJ]]
[[Category: Healy MD]]
[[Category: Heesom KJ]]
[[Category: Kadapalakere SY]]
[[Category: Kato K]]
[[Category: McConville C]]
[[Category: McNally KE]]
[[Category: Moody ERR]]
[[Category: Nguyen THD]]
[[Category: Palmer CS]]
[[Category: Planelles-Herrero VJ]]
[[Category: Ross J]]
[[Category: Sacharz J]]
[[Category: Saitoh S]]
[[Category: Shaw S]]
[[Category: Stroud DA]]
[[Category: Williams TA]]

Latest revision as of 09:41, 19 June 2024

Human CCC complexHuman CCC complex

Structural highlights

8f2r is a 10 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 3.12Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COMD1_HUMAN Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.[1] [2] [3] [4] [5] [6] [7]

References

  1. ↑ Burstein E, Ganesh L, Dick RD, van De Sluis B, Wilkinson JC, Klomp LW, Wijmenga C, Brewer GJ, Nabel GJ, Duckett CS. A novel role for XIAP in copper homeostasis through regulation of MURR1. EMBO J. 2004 Jan 14;23(1):244-54. Epub 2003 Dec 18. PMID:14685266 doi:10.1038/sj.emboj.7600031
  2. ↑ Burstein E, Hoberg JE, Wilkinson AS, Rumble JM, Csomos RA, Komarck CM, Maine GN, Wilkinson JC, Mayo MW, Duckett CS. COMMD proteins, a novel family of structural and functional homologs of MURR1. J Biol Chem. 2005 Jun 10;280(23):22222-32. Epub 2005 Mar 30. PMID:15799966 doi:http://dx.doi.org/10.1074/jbc.M501928200
  3. ↑ de Bie P, van de Sluis B, Burstein E, Duran KJ, Berger R, Duckett CS, Wijmenga C, Klomp LW. Characterization of COMMD protein-protein interactions in NF-kappaB signalling. Biochem J. 2006 Aug 15;398(1):63-71. PMID:16573520 doi:http://dx.doi.org/BJ20051664
  4. ↑ Narindrasorasak S, Kulkarni P, Deschamps P, She YM, Sarkar B. Characterization and copper binding properties of human COMMD1 (MURR1). Biochemistry. 2007 Mar 20;46(11):3116-28. Epub 2007 Feb 20. PMID:17309234 doi:http://dx.doi.org/10.1021/bi0620656
  5. ↑ Maine GN, Mao X, Komarck CM, Burstein E. COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase. EMBO J. 2007 Jan 24;26(2):436-47. Epub 2006 Dec 21. PMID:17183367 doi:http://dx.doi.org/10.1038/sj.emboj.7601489
  6. ↑ Thoms HC, Loveridge CJ, Simpson J, Clipson A, Reinhardt K, Dunlop MG, Stark LA. Nucleolar targeting of RelA(p65) is regulated by COMMD1-dependent ubiquitination. Cancer Res. 2010 Jan 1;70(1):139-49. doi: 10.1158/0008-5472.CAN-09-1397. PMID:20048074 doi:http://dx.doi.org/10.1158/0008-5472.CAN-09-1397
  7. ↑ Vonk WI, Wijmenga C, Berger R, van de Sluis B, Klomp LW. Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1. J Biol Chem. 2010 Sep 10;285(37):28991-9000. doi: 10.1074/jbc.M110.101477. Epub, 2010 Jul 1. PMID:20595380 doi:http://dx.doi.org/10.1074/jbc.M110.101477

8f2r, resolution 3.12Å

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