The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding
Open accessAbstract
SUMMARY STING is an essential signaling molecule for DNA and cyclic di-GMP (c-di-GMP)-mediated type I interferon (IFN) production via TANK-binding kinase 1 (TBK1) and Interferon regulatory factor 3 (IRF3) pathway. It contains an N-terminal transmembrane region and a cytosolic C-terminal domain (CTD). Here, we describe crystal structures of STING CTD alone and complexed with c-di-GMP in a unique binding mode. The strictly conserved AA153-173 region was shown to be cytosolic and participated in dimerization via hydrophobic interactions. The STING CTD functions as a dimer and the dimerization was independent of post-translational modifications. Binding of c-di-GMP enhanced interaction of a shorter construct of STING CTD (residues 139-344) with TBK1. This suggests an extra TBK1 binding site, other than Ser358. This study provides a glimpse into the unique architecture of STING and sheds new light on the mechanism of c-di-GMP-mediated TBK1 signaling.
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Metadata
- Authors
- Ouyang, S., Song, X., Wang, Y., Ru, H., Shaw, N., Jiang, Y., Niu, F., Zhu, Y., Qiu, W., Parvatiyar, K., Li, Y., Zhang, R., Cheng, G., & Liu, Z.-J.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 36
- Issue
- 6
- Pages
- 1073-1086
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2093268266
- Cited by
- 350
- References
- 10
- FWCI
- 10.48
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Ouyang, S., Song, X., Wang, Y., Ru, H., Shaw, N., Jiang, Y., Niu, F., Zhu, Y., Qiu, W., Parvatiyar, K., Li, Y., Zhang, R., Cheng, G., & Liu, Z.-J. (2012). Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding. Immunity. https://doi.org/10.1016/j.immuni.2012.03.019
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