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

Tian Y, Yin Q
Acta Crystallogr F Struct Biol Commun 75 455-460 (2019)
Cited: 6 times
EuropePMC logo PMID: 31204693

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.

Articles - 6oe9 mentioned but not cited (2)

  1. Structural analysis of the HIN1 domain of interferon-inducible protein 204. Tian Y, Yin Q. Acta Crystallogr F Struct Biol Commun 75 455-460 (2019)
  2. Structural mechanism of DNA recognition by the p204 HIN domain. Fan X, Jiang J, Zhao D, Chen F, Ma H, Smith P, Unterholzner L, Xiao TS, Jin T. Nucleic Acids Res 49 2959-2972 (2021)


Reviews citing this publication (4)

  1. Immunobiology and structural biology of AIM2 inflammasome. Wang B, Bhattacharya M, Roy S, Tian Y, Yin Q. Mol Aspects Med 76 100869 (2020)
  2. Interrogating Host Antiviral Environments Driven by Nuclear DNA Sensing: A Multiomic Perspective. Howard TR, Cristea IM. Biomolecules 10 E1591 (2020)
  3. Activation and Immune Regulation Mechanisms of PYHIN Family During Microbial Infection. Fan X, Jiao L, Jin T. Front Microbiol 12 809412 (2021)
  4. The role of inflammasomes in human diseases and their potential as therapeutic targets. Yao J, Sterling K, Wang Z, Zhang Y, Song W. Signal Transduct Target Ther 9 10 (2024)


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