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

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.

journal_name

Nat Struct Mol Biol

authors

Shang G,Zhu D,Li N,Zhang J,Zhu C,Lu D,Liu C,Yu Q,Zhao Y,Xu S,Gu L

doi

10.1038/nsmb.2332

subject

Has Abstract

pub_date

2012-06-24 00:00:00

pages

725-7

issue

7

eissn

1545-9993

issn

1545-9985

pii

nsmb.2332

journal_volume

19

pub_type

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