4a1s: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:


==Crystallographic structure of the Pins:Insc complex==
==Crystallographic structure of the Pins:Insc complex==
<StructureSection load='4a1s' size='340' side='right' caption='[[4a1s]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4a1s' size='340' side='right'caption='[[4a1s]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== 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>
<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>
Line 21: Line 21:
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Drome]]
[[Category: Large Structures]]
[[Category: Alfieri, A]]
[[Category: Alfieri, A]]
[[Category: Culurgioni, S]]
[[Category: Culurgioni, S]]

Revision as of 09:15, 16 October 2019

Crystallographic structure of the Pins:Insc complexCrystallographic structure of the Pins:Insc complex

Structural highlights

4a1s is a 4 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Culurgioni S, Alfieri A, Pendolino V, Laddomada F, Mapelli M. Inscuteable and NuMA proteins bind competitively to Leu-Gly-Asn repeat-enriched protein (LGN) during asymmetric cell divisions. Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):20998-1003. Epub 2011 Dec 14. PMID:22171003 doi:10.1073/pnas.1113077108

4a1s, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA