8Z37 | pdb_00008z37

Crystal structure of human STING ligand binding domain.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 
    0.245 (Depositor), 0.244 (DCC) 
  • R-Value Work: 
    0.220 (Depositor), 0.224 (DCC) 
  • R-Value Observed: 
    0.221 (Depositor) 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

A fluorescent STING ligand sensor for high-throughput screening of compounds that can enhance tumor immunotherapy.

Sun, P.Wang, B.Liu, C.Wang, Z.Liu, Y.Qiao, Y.B.Li, X.

(2025) Cell Rep Methods 5: 101106-101106

  • DOI: https://doi.org/10.1016/j.crmeth.2025.101106
  • Primary Citation of Related Structures:  
    8Z37

  • PubMed Abstract: 

    The activation of the stimulator of interferon genes (STING) pathway triggers the release of type I interferons that can potentiate the host immune response against tumors. STING agonism is therefore a promising strategy for the development of cancer immunotherapy; however, sensitive tools and assays for the discovery of STING modulators are currently limited. Here, we develop and characterize a STING ligand sensor, FiSL, to detect STING ligands in vitro. Utilizing FiSL, we identify honokiol, a natural compound derived from Magnolia species, as an orally available STING agonist from a bioactive compound library. Functional studies reveal that honokiol exerts antitumor activity in a STING-dependent manner. Moreover, in STING-humanized mouse tumor models, honokiol enhances the efficacy of anti-PD-(L)1 immunotherapy. Collectively, we have developed FiSL as a tool for high-throughput screening of STING ligands and revealed honokiol as a STING agonist that can be harnessed to treat human cancer.


  • Organizational Affiliation
    • Shanxi Key Laboratory of Innovative Drug for the Treatment of Serious Diseases Basing on the Chronic Inflammation, Shanxi University of Chinese Medicine, Jinzhong 030619, China; State Key Laboratory of Epigenetic Regulation and Intervention, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Stimulator of interferon genes protein192Homo sapiensMutation(s): 0 
Gene Names: STING1ERISMITASTINGTMEM173
UniProt & NIH Common Fund Data Resources
Find proteins for Q86WV6 (Homo sapiens)
Explore Q86WV6 
Go to UniProtKB:  Q86WV6
PHAROS:  Q86WV6
GTEx:  ENSG00000184584 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ86WV6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free:  0.245 (Depositor), 0.244 (DCC) 
  • R-Value Work:  0.220 (Depositor), 0.224 (DCC) 
  • R-Value Observed: 0.221 (Depositor) 
Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.714α = 90
b = 89.477β = 90
c = 72.955γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata scaling
XDSdata reduction
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China92157104

Revision History  (Full details and data files)

  • Version 1.0: 2025-04-16
    Type: Initial release
  • Version 1.1: 2025-10-22
    Changes: Database references