2h2m

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{{Seed}}
 
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[[Image:2h2m.png|left|200px]]
 
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==Solution Structure of the N-terminal domain of COMMD1 (Murr1)==
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The line below this paragraph, containing "STRUCTURE_2h2m", creates the "Structure Box" on the page.
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<StructureSection load='2h2m' size='340' side='right'caption='[[2h2m]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2h2m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_2h2m| PDB=2h2m | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h2m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Solution Structure of the N-terminal domain of COMMD1 (Murr1)===
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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<ref>PMID:17097678</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17097678}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2h2m" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17097678 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17097678}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2H2M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2M OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17097678 17097678]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Rosenzweig, A C.]]
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[[Category: Rosenzweig AC]]
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[[Category: Sommerhalter, M.]]
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[[Category: Sommerhalter M]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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[[Category: All alpha-helical]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:56:59 2008''
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Current revision

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

PDB ID 2h2m

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