1HQ8

CRYSTAL STRUCTURE OF THE MURINE NK CELL-ACTIVATING RECEPTOR NKG2D AT 1.95 A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.215 

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This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95 A.

Wolan, D.W.Teyton, L.Rudolph, M.G.Villmow, B.Bauer, S.Busch, D.H.Wilson, I.A.

(2001) Nat Immunol 2: 248-254

  • DOI: https://doi.org/10.1038/85311
  • Primary Citation of Related Structures:  
    1HQ8

  • PubMed Abstract: 

    NKG2D, a homodimeric lectin-like receptor, is a unique stimulatory molecule that is found on natural killer cells,T cells and activated macrophages. The natural ligands for murine NKG2D are distant major histocompatibility complex homologs, retinoic acid early transcript (Rae1) and H-60 minor histocompatibility antigen. The crystal structure of the extracellular region of murine NKG2D reveals close homology with other C-type lectin receptors such as CD94, Ly49A, rat MBP-A and CD69. However, the precise mode of dimeric assembly varies among these natural killer receptors, as well as their surface topography and electrostatic properties. The NKG2D structure provides the first structural insights into the role and ligand specificity of this stimulatory receptor in the innate and adaptive immune system.


  • Organizational Affiliation

    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NKG2-D123Mus musculusMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for O54709 (Mus musculus)
Explore O54709 
Go to UniProtKB:  O54709
IMPC:  MGI:1196250
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO54709
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.215 
  • Space Group: I 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.86α = 90
b = 85.19β = 90
c = 87.58γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-03-07
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance