The structural basis for the sensing and binding of cyclic di-GMP by STING.
STING (stimulator of interferon genes) is an essential signaling adaptor that mediates cytokine production in response to microbial invasion by directly sensing bacterial secondary messengers such as the cyclic dinucleotide bis-(3'-5')-cyclic dimeric GMP (c-di-GMP). STING's structure and its binding mechanism to cyclic dinucleotides were unknown. We report here the crystal structures of the STING cytoplasmic domain and its complex with c-di-GMP, thus providing the structural basis for understanding STING function.
State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Yi-He
YH
Huang
Xiang-Yu
XY
Liu
Xiao-Xia
XX
Du
Zheng-Fan
ZF
Jiang
Xiao-Dong
XD
Su
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D000099197:STING Protein
D006152:Cyclic GMP; D008565:Membrane Proteins; C532857:STING1 protein, human; D000099197:STING Protein; C062025:bis(3',5')-cyclic diguanylic acid