4a1s: Difference between revisions
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==Crystallographic structure of the Pins:Insc complex== | |||
<StructureSection load='4a1s' size='340' side='right' caption='[[4a1s]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a1s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A1S FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=4a1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a1s OCA], [http://pdbe.org/4a1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a1s RCSB], [http://www.ebi.ac.uk/pdbsum/4a1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a1s ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Coupling of spindle orientation to cellular polarity is a prerequisite for epithelial asymmetric cell divisions. The current view posits that the adaptor Inscuteable (Insc) bridges between Par3 and the spindle tethering machinery assembled on NuMALGNGalphai(GDP), thus triggering apico-basal spindle orientation. The crystal structure of the Drosophila ortholog of LGN (known as Pins) in complex with Insc reveals a modular interface contributed by evolutionary conserved residues. The structure also identifies a positively charged patch of LGN binding to an invariant EPE-motif present on both Insc and NuMA. In vitro competition assays indicate that Insc competes with NuMA for LGN binding, displaying a higher affinity, and that it is capable of opening the LGN conformational switch. The finding that Insc and NuMA are mutually exclusive interactors of LGN challenges the established model of force generators assembly, which we revise on the basis of the newly discovered biochemical properties of the intervening components. | |||
Inscuteable and NuMA proteins bind competitively to Leu-Gly-Asn repeat-enriched protein (LGN) during asymmetric cell divisions.,Culurgioni S, Alfieri A, Pendolino V, Laddomada F, Mapelli M Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):20998-1003. Epub 2011 Dec 14. PMID:22171003<ref>PMID:22171003</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a1s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Drome]] | ||
[[Category: Alfieri, A | [[Category: Alfieri, A]] | ||
[[Category: Culurgioni, S | [[Category: Culurgioni, S]] | ||
[[Category: Laddomada, F | [[Category: Laddomada, F]] | ||
[[Category: Mapelli, M | [[Category: Mapelli, M]] | ||
[[Category: Pendolino, V | [[Category: Pendolino, V]] | ||
[[Category: Asymmetric cell division]] | [[Category: Asymmetric cell division]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Lgn]] | [[Category: Lgn]] | ||
[[Category: Mitotic spindle orientation]] | [[Category: Mitotic spindle orientation]] | ||
Revision as of 18:31, 5 August 2016
Crystallographic structure of the Pins:Insc complexCrystallographic structure of the Pins:Insc complex
Structural highlights
Publication Abstract from PubMedCoupling of spindle orientation to cellular polarity is a prerequisite for epithelial asymmetric cell divisions. The current view posits that the adaptor Inscuteable (Insc) bridges between Par3 and the spindle tethering machinery assembled on NuMALGNGalphai(GDP), thus triggering apico-basal spindle orientation. The crystal structure of the Drosophila ortholog of LGN (known as Pins) in complex with Insc reveals a modular interface contributed by evolutionary conserved residues. The structure also identifies a positively charged patch of LGN binding to an invariant EPE-motif present on both Insc and NuMA. In vitro competition assays indicate that Insc competes with NuMA for LGN binding, displaying a higher affinity, and that it is capable of opening the LGN conformational switch. The finding that Insc and NuMA are mutually exclusive interactors of LGN challenges the established model of force generators assembly, which we revise on the basis of the newly discovered biochemical properties of the intervening components. Inscuteable and NuMA proteins bind competitively to Leu-Gly-Asn repeat-enriched protein (LGN) during asymmetric cell divisions.,Culurgioni S, Alfieri A, Pendolino V, Laddomada F, Mapelli M Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):20998-1003. Epub 2011 Dec 14. PMID:22171003[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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