View source for 9c72


==Structure of the ASH3 domain of Drosophila melanogaster Spd-2==
<StructureSection load='9c72' size='340' side='right'caption='[[9c72]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9c72]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9C72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C72 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9c72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c72 OCA], [https://pdbe.org/9c72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c72 RCSB], [https://www.ebi.ac.uk/pdbsum/9c72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c72 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9c72" 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]]