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. [ABSTRACT FROM AUTHOR]