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| | ==The crystal structure of the n-terminal domain of COMMD9== | | ==The crystal structure of the n-terminal domain of COMMD9== |
| - | <StructureSection load='4oe9' size='340' side='right' caption='[[4oe9]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='4oe9' size='340' side='right'caption='[[4oe9]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oe9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OE9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oe9]] is a 2 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=4OE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OE9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4oe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oe9 OCA], [https://pdbe.org/4oe9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oe9 RCSB], [https://www.ebi.ac.uk/pdbsum/4oe9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oe9 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h2m|2h2m]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COMMD9, HSPC166 ([http://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=4oe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oe9 OCA], [http://pdbe.org/4oe9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oe9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oe9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oe9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/COMD9_HUMAN COMD9_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Celligoi, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Hospenthal, M]] | + | [[Category: Celligoi D]] |
| - | [[Category: Lott, J S]] | + | [[Category: Hospenthal M]] |
| - | [[Category: All alpha helical]] | + | [[Category: Lott JS]] |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
COMD9_HUMAN
Publication Abstract from PubMed
The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which is localized to endosomal compartments and mediates the transport of several transmembrane cargos. How these complexes are formed however is completely unknown. Here, we have systematically characterised the interactions between human COMMD proteins, and determined structures of COMMD proteins using X-ray crystallography and X-ray scattering to provide insights into the underlying mechanisms of homo- and heteromeric assembly. All COMMD proteins possess an alpha-helical N-terminal domain, and a highly conserved C-terminal domain that forms a tightly interlocked dimeric structure responsible for COMMD-COMMD interactions. The COMM domains also bind directly to components of CCC and mediate non-specific membrane association. Overall these studies show that COMMD proteins function as obligatory dimers with conserved domain architectures.
Structural insights into the architecture and membrane interactions of the conserved COMMD proteins.,Healy MD, Hospenthal MK, Hall RJ, Chandra M, Chilton M, Tillu V, Chen KE, Celligoi DJ, McDonald FJ, Cullen PJ, Lott JS, Collins BM, Ghai R Elife. 2018 Aug 1;7. pii: 35898. doi: 10.7554/eLife.35898. PMID:30067224[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Healy MD, Hospenthal MK, Hall RJ, Chandra M, Chilton M, Tillu V, Chen KE, Celligoi DJ, McDonald FJ, Cullen PJ, Lott JS, Collins BM, Ghai R. Structural insights into the architecture and membrane interactions of the conserved COMMD proteins. Elife. 2018 Aug 1;7. pii: 35898. doi: 10.7554/eLife.35898. PMID:30067224 doi:http://dx.doi.org/10.7554/eLife.35898
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