4A1S

Crystallographic structure of the Pins:Insc complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.208 
  • R-Value Observed: 0.210 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

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.

(2011) Proc Natl Acad Sci U S A 108: 20998

  • DOI: https://doi.org/10.1073/pnas.1113077108
  • Primary Citation of Related Structures:  
    4A1S

  • 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.


  • Organizational Affiliation

    Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PARTNER OF INSCUTEABLE
A, B
411Drosophila melanogasterMutation(s): 0 
UniProt
Find proteins for Q9VB22 (Drosophila melanogaster)
Explore Q9VB22 
Go to UniProtKB:  Q9VB22
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9VB22
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
RE60102PC,
D [auth E]
40Drosophila melanogasterMutation(s): 0 
UniProt
Find proteins for Q9W2R4 (Drosophila melanogaster)
Explore Q9W2R4 
Go to UniProtKB:  Q9W2R4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9W2R4
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.208 
  • R-Value Observed: 0.210 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 160.2α = 90
b = 64.232β = 117.9
c = 107.599γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
SCALEPACKdata scaling
SHELXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-03-28
    Type: Initial release
  • Version 1.1: 2012-11-07
    Changes: Database references
  • Version 1.2: 2019-10-16
    Changes: Data collection, Experimental preparation, Other
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references