9fu8
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the ASH1 domain of Drosophila melanogaster Spd-2== | |
| + | <StructureSection load='9fu8' size='340' side='right'caption='[[9fu8]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9fu8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FU8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=9fu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fu8 OCA], [https://pdbe.org/9fu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fu8 RCSB], [https://www.ebi.ac.uk/pdbsum/9fu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fu8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9VV79_DROME Q9VV79_DROME] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Centrosomes form when centrioles assemble pericentriolar material (PCM) around themselves. Spd-2/CEP192 proteins, defined by a conserved "Spd-2 domain" (SP2D) comprising two closely spaced AspM-Spd-2-Hydin (ASH) domains, play a critical role in centrosome assembly. Here, we show that the SP2D does not target Drosophila Spd-2 to centrosomes but rather promotes PCM scaffold assembly. Crystal structures of the human and honeybee SP2D reveal an unusual "extended cradle" structure mediated by a conserved interaction interface between the two ASH domains. Mutations predicted to perturb this interface, including a human mutation associated with male infertility and Mosaic Variegated Aneuploidy, disrupt PCM scaffold assembly in flies. The SP2D is monomeric in solution, but the Drosophila SP2D can form higher-order oligomers upon phosphorylation by PLK1 (Polo-like kinase 1). Crystal-packing interactions and AlphaFold predictions suggest how SP2Ds might self-assemble, and mutations associated with one such potential dimerization interface markedly perturb SP2D oligomerization in vitro and PCM scaffold assembly in vivo. | ||
| - | + | The conserved Spd-2/CEP192 domain adopts a unique protein fold to promote centrosome scaffold assembly.,Hu L, Wainman A, Andreeva A, Apizi M, Alvarez-Rodrigo I, Wong SS, Saurya S, Sheppard D, Cottee M, Johnson S, Lea SM, Raff JW, van Breugel M, Feng Z Sci Adv. 2025 Mar 21;11(12):eadr5744. doi: 10.1126/sciadv.adr5744. Epub 2025 Mar , 19. PMID:40106572<ref>PMID:40106572</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9fu8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Feng Z]] | ||
| + | [[Category: Johnson S]] | ||
| + | [[Category: Lea SM]] | ||
| + | [[Category: Raff JW]] | ||
| + | [[Category: Sheppard D]] | ||
Current revision
Structure of the ASH1 domain of Drosophila melanogaster Spd-2
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