5cff: Difference between revisions
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==Crystal structure of Miranda/Staufen dsRBD5 complex== | |||
<StructureSection load='5cff' size='340' side='right'caption='[[5cff]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cff]] is a 8 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=5CFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CFF 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]] 2.5Å</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=5cff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cff OCA], [https://pdbe.org/5cff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cff RCSB], [https://www.ebi.ac.uk/pdbsum/5cff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cff ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9VDR7_DROME Q9VDR7_DROME] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
During the asymmetric division of Drosophila neuroblasts (NBs), the scaffold Miranda (Mira) coordinates the subcellular distribution of cell-fate determinants including Staufen (Stau) and segregates them into the ganglion mother cells (GMCs). Here we show the fifth double-stranded RNA (dsRNA)-binding domain (dsRBD5) of Stau is necessary and sufficient for binding to a coiled-coil region of Mira cargo-binding domain (CBD). The crystal structure of Mira514-595/Stau dsRBD5 complex illustrates that Mira forms an elongated parallel coiled-coil dimer, and two dsRBD5 symmetrically bind to the Mira dimer through their exposed beta-sheet faces, revealing a previously unrecognized protein interaction mode for dsRBDs. We further demonstrate that the Mira-Stau dsRBD5 interaction is responsible for the asymmetric localization of Stau during Drosophila NB asymmetric divisions. Finally, we find the CBD-mediated dimer assembly is likely a common requirement for Mira to recognize and translocate other cargos including brain tumour (Brat). | |||
The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division.,Jia M, Shan Z, Yang Y, Liu C, Li J, Luo ZG, Zhang M, Cai Y, Wen W, Wang W Nat Commun. 2015 Oct 1;6:8381. doi: 10.1038/ncomms9381. PMID:26423004<ref>PMID:26423004</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5cff" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | |||
[[Category: Shan Z]] | |||
[[Category: Wen W]] | |||
Latest revision as of 11:46, 23 October 2024
Crystal structure of Miranda/Staufen dsRBD5 complexCrystal structure of Miranda/Staufen dsRBD5 complex
Structural highlights
FunctionPublication Abstract from PubMedDuring the asymmetric division of Drosophila neuroblasts (NBs), the scaffold Miranda (Mira) coordinates the subcellular distribution of cell-fate determinants including Staufen (Stau) and segregates them into the ganglion mother cells (GMCs). Here we show the fifth double-stranded RNA (dsRNA)-binding domain (dsRBD5) of Stau is necessary and sufficient for binding to a coiled-coil region of Mira cargo-binding domain (CBD). The crystal structure of Mira514-595/Stau dsRBD5 complex illustrates that Mira forms an elongated parallel coiled-coil dimer, and two dsRBD5 symmetrically bind to the Mira dimer through their exposed beta-sheet faces, revealing a previously unrecognized protein interaction mode for dsRBDs. We further demonstrate that the Mira-Stau dsRBD5 interaction is responsible for the asymmetric localization of Stau during Drosophila NB asymmetric divisions. Finally, we find the CBD-mediated dimer assembly is likely a common requirement for Mira to recognize and translocate other cargos including brain tumour (Brat). The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division.,Jia M, Shan Z, Yang Y, Liu C, Li J, Luo ZG, Zhang M, Cai Y, Wen W, Wang W Nat Commun. 2015 Oct 1;6:8381. doi: 10.1038/ncomms9381. PMID:26423004[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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