Structural analysis of the HIN1 domain of interferon-inducible protein 204

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.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: interferon-inducible protein 204 p204 HIN domain DNA binding research communications Source Type: research

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