6OE9

Crystal structure of p204 HIN1 domain

Summary for 6OE9

• Entry DOI: 10.2210/pdb6oe9/pdb
• Related: 2OQ0 4L5Q 4L5R 4L5s 5YZP 5Z7D
• Descriptor: Interferon-activable protein 204, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: dna binding protein, cytosolic protein, immune system
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 23888.15

Authors

Tian, Y.,Yin, Q. (deposition date: 2019-03-27, release date: 2019-07-10, Last modification date: 2023-10-11)

Primary citation

Tian, Y.,Yin, Q.
Structural analysis of the HIN1 domain of interferon-inducible protein 204.
Acta Crystallogr.,Sect.F, 75:455-460, 2019

PubMed 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.

PubMed: 31204693
DOI: 10.1107/S2053230X19007167

Experimental method

X-RAY DIFFRACTION (1.94 Å)