干扰素诱导蛋白204的HIN1结构域的结构分析。
Structural analysis of the HIN1 domain of interferon-inducible protein 204.
作者信息
Tian Yuan, Yin Qian
机构信息
Department of Biological Science, Florida State University, Tallahassee, FL 32306, USA.
出版信息
Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):455-460. doi: 10.1107/S2053230X19007167. Epub 2019 Jun 10.
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.
摘要
干扰素诱导蛋白204（p204）与微生物DNA结合以引发炎症反应并诱导干扰素产生。p204还通过调节各种转录因子来调控细胞增殖和分化。p204中的C末端HIN结构域被认为负责DNA结合，但其结合模式尚未完全了解。已对p204 HIN1结构域的DNA结合亲和力进行了表征，并确定了其晶体结构，从而深入了解其与DNA的相互作用。表面电荷分布以及序列比对表明，p204 HIN结构域利用其L12和L45环进行DNA结合。
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