4A1S

Crystallographic structure of the Pins:Insc complex

4A1S の概要

• エントリーDOI: 10.2210/pdb4a1s/pdb
• 分子名称: PARTNER OF INSCUTEABLE, RE60102P (3 entities in total)
• 機能のキーワード: cell cycle, lgn, mitotic spindle orientation, asymmetric cell divisions
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96880.58

構造登録者

Culurgioni, S.,Alfieri, A.,Pendolino, V.,Laddomada, F.,Mapelli, M. (登録日: 2011-09-19, 公開日: 2012-03-28, 最終更新日: 2024-05-08)

主引用文献

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.USA, 108:20998-, 2011

PubMed Abstract: 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 NuMALGNGαi(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.

PubMed: 22171003
DOI: 10.1073/PNAS.1113077108

実験手法

X-RAY DIFFRACTION (2.1 Å)