Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System

STING, stimulator of interferon genes, is an innate immune sensor of cyclic dinucleotides that regulates the induction of type I interferons. STING C-terminal domain forms a V-shaped dimer and binds a c-di-GMP molecule at the dimer interface through direct and solvent-mediated hydrogen bonds. The gu...

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Autores principales: Shu, Chang, Yi, Guanghui, Watts, Tylan, Kao, C. Cheng, Li, Pingwei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3392545/
https://www.ncbi.nlm.nih.gov/pubmed/22728658
http://dx.doi.org/10.1038/nsmb.2331
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author Shu, Chang
Yi, Guanghui
Watts, Tylan
Kao, C. Cheng
Li, Pingwei
author_facet Shu, Chang
Yi, Guanghui
Watts, Tylan
Kao, C. Cheng
Li, Pingwei
author_sort Shu, Chang
collection PubMed
description STING, stimulator of interferon genes, is an innate immune sensor of cyclic dinucleotides that regulates the induction of type I interferons. STING C-terminal domain forms a V-shaped dimer and binds a c-di-GMP molecule at the dimer interface through direct and solvent-mediated hydrogen bonds. The guanine bases of c-di-GMP stack against the phenolic rings of a conserved tyrosine residue. Mutations at the c-di-GMP binding surface reduce nucleotide binding and affect signaling.
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spelling pubmed-33925452013-01-01 Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System Shu, Chang Yi, Guanghui Watts, Tylan Kao, C. Cheng Li, Pingwei Nat Struct Mol Biol Article STING, stimulator of interferon genes, is an innate immune sensor of cyclic dinucleotides that regulates the induction of type I interferons. STING C-terminal domain forms a V-shaped dimer and binds a c-di-GMP molecule at the dimer interface through direct and solvent-mediated hydrogen bonds. The guanine bases of c-di-GMP stack against the phenolic rings of a conserved tyrosine residue. Mutations at the c-di-GMP binding surface reduce nucleotide binding and affect signaling. 2012-06-24 /pmc/articles/PMC3392545/ /pubmed/22728658 http://dx.doi.org/10.1038/nsmb.2331 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Shu, Chang
Yi, Guanghui
Watts, Tylan
Kao, C. Cheng
Li, Pingwei
Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System
title Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System
title_full Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System
title_fullStr Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System
title_full_unstemmed Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System
title_short Structure of STING bound to c-di-GMP Reveals the Mechanism of Cyclic Dinucleotide Recognition by the Immune System
title_sort structure of sting bound to c-di-gmp reveals the mechanism of cyclic dinucleotide recognition by the immune system
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3392545/
https://www.ncbi.nlm.nih.gov/pubmed/22728658
http://dx.doi.org/10.1038/nsmb.2331
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