8GJZ

Structure of a STING receptor from S. pistillata Sp-STING1 bound to 2'3'-cUA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.92 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.198 

Starting Model: experimental
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This is version 1.3 of the entry. See complete history


Literature

cGLRs are a diverse family of pattern recognition receptors in innate immunity.

Li, Y.Slavik, K.M.Toyoda, H.C.Morehouse, B.R.de Oliveira Mann, C.C.Elek, A.Levy, S.Wang, Z.Mears, K.S.Liu, J.Kashin, D.Guo, X.Mass, T.Sebe-Pedros, A.Schwede, F.Kranzusch, P.J.

(2023) Cell 186: 3261-3276.e20

  • DOI: https://doi.org/10.1016/j.cell.2023.05.038
  • Primary Citation of Related Structures:  
    8EFM, 8EFN, 8GJW, 8GJX, 8GJY, 8GJZ

  • PubMed Abstract: 

    Cyclic GMP-AMP synthase (cGAS) is an enzyme in human cells that controls an immune response to cytosolic DNA. Upon binding DNA, cGAS synthesizes a nucleotide signal 2'3'-cGAMP that activates STING-dependent downstream immunity. Here, we discover that cGAS-like receptors (cGLRs) constitute a major family of pattern recognition receptors in innate immunity. Building on recent analysis in Drosophila, we identify >3,000 cGLRs present in nearly all metazoan phyla. A forward biochemical screening of 150 animal cGLRs reveals a conserved mechanism of signaling including response to dsDNA and dsRNA ligands and synthesis of isomers of the nucleotide signals cGAMP, c-UMP-AMP, and c-di-AMP. Combining structural biology and in vivo analysis in coral and oyster animals, we explain how synthesis of distinct nucleotide signals enables cells to control discrete cGLR-STING signaling pathways. Our results reveal cGLRs as a widespread family of pattern recognition receptors and establish molecular rules that govern nucleotide signaling in animal immunity.


  • Organizational Affiliation

    Department of Microbiology, Harvard Medical School, Boston, MA 02115, USA; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA 02115, USA; Parker Institute for Cancer Immunotherapy at Dana-Farber Cancer Institute, Boston, MA 02115, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Stimulator of interferon genes protein
A, B
188Stylophora pistillataMutation(s): 0 
Gene Names: Tmem173
UniProt
Find proteins for A0A2B4SJD2 (Stylophora pistillata)
Explore A0A2B4SJD2 
Go to UniProtKB:  A0A2B4SJD2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A2B4SJD2
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZNT (Subject of Investigation/LOI)
Query on ZNT

Download Ideal Coordinates CCD File 
C [auth A]2'3'-cUA
C19 H23 N7 O14 P2
QFSRDWZEQDGHEV-KPKSGTNCSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.92 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.198 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 113.429α = 90
b = 113.429β = 90
c = 259.272γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
AutoSolphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United States1DP2GM146250-01

Revision History  (Full details and data files)

  • Version 1.0: 2023-07-05
    Type: Initial release
  • Version 1.1: 2023-07-12
    Changes: Database references
  • Version 1.2: 2023-08-02
    Changes: Database references
  • Version 1.3: 2024-11-13
    Changes: Data collection, Structure summary