Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP.
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.
State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, China.
Guijun
G
Shang
Deyu
D
Zhu
Ning
N
Li
Junbing
J
Zhang
Chunyuan
C
Zhu
Defen
D
Lu
Cuilan
C
Liu
Qian
Q
Yu
Yanyu
Y
Zhao
Sujuan
S
Xu
Lichuan
L
Gu
D006152:Cyclic GMP / Q000031:analogs & derivatives; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D000099197:STING Protein
D006152:Cyclic GMP; D008565:Membrane Proteins; C532857:STING1 protein, human; D000099197:STING Protein; C062025:bis(3',5')-cyclic diguanylic acid