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• W2952122713 abstract "Interferon-inducible protein 204 (p204) binds to microbial DNA to elicit inflammatory responses and induce interferon production. p204 also modulates cell proliferation and differentiation by regulating various transcription factors. The C-terminal HIN domains in p204 are believed to be responsible for DNA binding, but the binding mode is not fully understood. The DNA-binding affinity of the p204 HIN1 domain has been characterized and its crystal structure has been determined, providing insight into its interaction with DNA. Surface-charge distribution together with sequence alignment suggests that the p204 HIN domain uses its L12 and L45 loops for DNA binding." @default.
• W2952122713 created "2019-06-27" @default.
• W2952122713 creator A5002083359 @default.
• W2952122713 creator A5008108176 @default.
• W2952122713 date "2019-06-01" @default.
• W2952122713 modified "2023-09-28" @default.
• W2952122713 title "Structural analysis of the HIN1 domain of interferon-inducible protein 204." @default.
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• W2952122713 doi "https://doi.org/10.2210/pdb6oe9/pdb" @default.
• W2952122713 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6572094" @default.
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• W2952122713 hasPublicationYear "2019" @default.
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