Display Settings:

Format

Send to:

Choose Destination
Nat Struct Mol Biol. 2012 Jun 24;19(7):725-7. doi: 10.1038/nsmb.2332.

Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP.

Author information

  • 1State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, China.

Abstract

STING functions as both an adaptor protein signaling cytoplasmic double-stranded DNA and a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal structures of the C-terminal domain of human STING (STING(CTD)) and its complex with c-di-GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface loops, which serve as a gate and latch of the cleft formed by the dimeric STING(CTD), undergo rearrangements to interact with the ligand.

PMID:
22728660
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Nature Publishing Group
    Loading ...
    Write to the Help Desk