8p0w: Difference between revisions

Revision as of 08:19, 20 March 2024

Structure of the human Commander complex COMMD ring

Structural highlights

8p0w 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 2.9Å
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

↑ 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
↑ 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:https://dx.doi.org/10.1074/jbc.M501928200
↑ 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:https://dx.doi.org/BJ20051664
↑ 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:https://dx.doi.org/10.1021/bi0620656
↑ 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:https://dx.doi.org/10.1038/sj.emboj.7601489
↑ 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:https://dx.doi.org/10.1158/0008-5472.CAN-09-1397
↑ 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:https://dx.doi.org/10.1074/jbc.M110.101477

Proteopedia Page Contributors and Editors (what is this?)

OCA

[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:https://dx.doi.org/10.1074/jbc.M501928200

[3] 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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.1074/jbc.M110.101477

[1]

[2]

[3]

[4]

[5]

[6]

[7]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8p0w is ON HOLD  until Paper Publication
+==Structure of the human Commander complex COMMD ring==
+<StructureSection load='8p0w' size='340' side='right'caption='[[8p0w]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-Authors: Kumpula, E.P., Laulumaa, S., Huiskonen, J.T.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8p0w]] 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=8P0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P0W FirstGlance]. <br>
-Description: Structure of the human Commander complex COMMD ring
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#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=8p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p0w OCA], [https://pdbe.org/8p0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p0w RCSB], [https://www.ebi.ac.uk/pdbsum/8p0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p0w ProSAT]</span></td></tr>
-[[Category: Kumpula, E.P]]
+</table>
-[[Category: Laulumaa, S]]
+== Function ==
-[[Category: Huiskonen, J.T]]
+[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: Huiskonen JT]]
+[[Category: Kumpula EP]]
+[[Category: Laulumaa S]]

8p0w: Difference between revisions

Revision as of 08:19, 20 March 2024

Structure of the human Commander complex COMMD ring

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools