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| | <StructureSection load='5oid' size='340' side='right'caption='[[5oid]], [[Resolution|resolution]] 4.60Å' scene=''> | | <StructureSection load='5oid' size='340' side='right'caption='[[5oid]], [[Resolution|resolution]] 4.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oid]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OID OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OID FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oid]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Trichoplax_adhaerens Trichoplax adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OID FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5oid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oid OCA], [http://pdbe.org/5oid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oid RCSB], [http://www.ebi.ac.uk/pdbsum/5oid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oid ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5oid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oid OCA], [https://pdbe.org/5oid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oid RCSB], [https://www.ebi.ac.uk/pdbsum/5oid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oid ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CEP85_HUMAN CEP85_HUMAN]] Acts as a negative regulator of NEK2 to maintain the centrosome integrity in interphase. Suppresses centrosome disjunction by inhibiting NEK2 kinase activity (PubMed:26220856).<ref>PMID:26220856</ref> | + | [https://www.uniprot.org/uniprot/B3S3X5_TRIAD B3S3X5_TRIAD] |
| | <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: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Breugel, M van]] | + | [[Category: Trichoplax adhaerens]] |
| - | [[Category: Centriole]] | + | [[Category: Van Breugel M]] |
| - | [[Category: Centrosome]]
| + | |
| - | [[Category: Cep85]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Stil]]
| + | |
| Structural highlights
Function
B3S3X5_TRIAD
Publication Abstract from PubMed
Centrosomes are required for faithful chromosome segregation during mitosis. They are composed of a centriole pair that recruits and organizes the microtubule-nucleating pericentriolar material. Centriole duplication is tightly controlled in vivo and aberrations in this process are associated with several human diseases, including cancer and microcephaly. Although factors essential for centriole assembly, such as STIL and PLK4, have been identified, the underlying molecular mechanisms that drive this process are incompletely understood. Combining protein proximity mapping with high-resolution structural methods, we identify CEP85 as a centriole duplication factor that directly interacts with STIL through a highly conserved interaction interface involving a previously uncharacterised domain of STIL. Structure-guided mutational analyses in vivo demonstrate that this interaction is essential for efficient centriolar targeting of STIL, PLK4 activation and faithful daughter centriole assembly. Taken together, our results illuminate a molecular mechanism underpinning the spatiotemporal regulation of the early stages of centriole duplication.
Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly.,Liu Y, Gupta GD, Barnabas DD, Agircan FG, Mehmood S, Wu D, Coyaud E, Johnson CM, McLaughlin SH, Andreeva A, Freund SMV, Robinson CV, Cheung SWT, Raught B, Pelletier L, van Breugel M Nat Commun. 2018 Apr 30;9(1):1731. doi: 10.1038/s41467-018-04122-x. PMID:29712910[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu Y, Gupta GD, Barnabas DD, Agircan FG, Mehmood S, Wu D, Coyaud E, Johnson CM, McLaughlin SH, Andreeva A, Freund SMV, Robinson CV, Cheung SWT, Raught B, Pelletier L, van Breugel M. Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly. Nat Commun. 2018 Apr 30;9(1):1731. doi: 10.1038/s41467-018-04122-x. PMID:29712910 doi:http://dx.doi.org/10.1038/s41467-018-04122-x
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