6QJA

Organizational principles of the NuMA-Dynein interaction interface and implications for mitotic spindle functions


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.54 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Organizational Principles of the NuMA-Dynein Interaction Interface and Implications for Mitotic Spindle Functions.

Renna, C.Rizzelli, F.Carminati, M.Gaddoni, C.Pirovano, L.Cecatiello, V.Pasqualato, S.Mapelli, M.

(2020) Structure 28: 820-829.e6

  • DOI: https://doi.org/10.1016/j.str.2020.04.017
  • Primary Citation of Related Structures:  
    6QJA

  • PubMed Abstract: 

    Mitotic progression is orchestrated by the microtubule-based motor dynein, which sustains all mitotic spindle functions. During cell division, cytoplasmic dynein acts with the high-molecular-weight complex dynactin and nuclear mitotic apparatus (NuMA) to organize and position the spindle. Here, we analyze the interaction interface between NuMA and the light intermediate chain (LIC) of eukaryotic dynein. Structural studies show that NuMA contains a hook domain contacting directly LIC1 and LIC2 chains through a conserved hydrophobic patch shared among other Hook adaptors. In addition, we identify a LIC-binding motif within the coiled-coil region of NuMA that is homologous to CC1-boxes. Analysis of mitotic cells revealed that both LIC-binding sites of NuMA are essential for correct spindle placement and cell division. Collectively, our evidence depicts NuMA as the dynein-activating adaptor acting in the mitotic processes of spindle organization and positioning.


  • Organizational Affiliation

    IEO, European Institute of Oncology IRCCS, 20141 Milan, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Nuclear mitotic apparatus protein 1
A, B, C, D
157Homo sapiensMutation(s): 0 
Gene Names: NUMA1NMP22NUMA
UniProt & NIH Common Fund Data Resources
Find proteins for Q14980 (Homo sapiens)
Explore Q14980 
Go to UniProtKB:  Q14980
PHAROS:  Q14980
GTEx:  ENSG00000137497 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ14980
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.54 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.73α = 90
b = 112.85β = 90
c = 135.81γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
xia2data reduction
xia2data scaling
PDB_EXTRACTdata extraction
xia2data reduction
AutoSolphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Italian Association for Cancer ResearchItalyIG 18629
Other governmentItalyRF-2013-02357254

Revision History  (Full details and data files)

  • Version 1.0: 2020-02-05
    Type: Initial release
  • Version 1.1: 2020-04-29
    Changes: Database references
  • Version 1.2: 2020-05-06
    Changes: Structure summary
  • Version 1.3: 2020-05-27
    Changes: Database references
  • Version 1.4: 2020-07-15
    Changes: Database references
  • Version 1.5: 2024-05-15
    Changes: Data collection, Database references, Refinement description