This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2h2m

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:29, 17 March 2021

Solution Structure of the N-terminal domain of COMMD1 (Murr1)

Structural highlights

2h2m is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	COMMD1 (HUMAN)
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

COMMD1 is the prototype of a new protein family that plays a role in several important cellular processes, including NF-kappaB signaling, sodium transport, and copper metabolism. The COMMD proteins interact with one another via a conserved C-terminal domain, whereas distinct functions are predicted to result from a variable N-terminal domain. The COMMD proteins have not been characterized biochemically or structurally. Here, we present the solution structure of the N-terminal domain of COMMD1 (N-COMMD1, residues 1-108). This domain adopts an alpha-helical structure that bears little resemblance to any other helical protein. The compact nature of N-COMMD1 suggests that full-length COMMD proteins are modular, consistent with specific functional properties for each domain. Interactions between N-COMMD1 and partner proteins may occur via complementary electrostatic surfaces. These data provide a new foundation for biochemical characterization of COMMD proteins and for probing COMMD1 protein-protein interactions at the molecular level.

Solution structure of the COMMD1 N-terminal domain.,Sommerhalter M, Zhang Y, Rosenzweig AC J Mol Biol. 2007 Jan 19;365(3):715-21. Epub 2006 Oct 13. PMID:17097678^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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:http://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:http://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:http://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:http://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:http://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:http://dx.doi.org/10.1074/jbc.M110.101477
↑ Sommerhalter M, Zhang Y, Rosenzweig AC. Solution structure of the COMMD1 N-terminal domain. J Mol Biol. 2007 Jan 19;365(3):715-21. Epub 2006 Oct 13. PMID:17097678 doi:10.1016/j.jmb.2006.10.030

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h2m"

@@ Line 1: / Line 1: @@
 ==Solution Structure of the N-terminal domain of COMMD1 (Murr1)==
-<StructureSection load='2h2m' size='340' side='right' caption='[[2h2m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2h2m' size='340' side='right'caption='[[2h2m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2h2m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H2M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2h2m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2M FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COMMD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COMMD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2h2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2m OCA], [http://pdbe.org/2h2m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h2m RCSB], [http://www.ebi.ac.uk/pdbsum/2h2m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2m ProSAT]</span></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=2h2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2m OCA], [https://pdbe.org/2h2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2m RCSB], [https://www.ebi.ac.uk/pdbsum/2h2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2m ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Rosenzweig, A C]]
 [[Category: Sommerhalter, M]]

2h2m

From Proteopedia

Revision as of 07:29, 17 March 2021

Solution Structure of the N-terminal domain of COMMD1 (Murr1)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox