13C and 15N resonance assignments of the DNA binding domain of interferon regulatory factor-3

被引：0
作者：
Nitin Dhaka [1 ]
Sunirmala Sahoo [2 ]
Biswajit Samal [1 ]
Sulakshana P. Mukherjee [1 ]
机构：
[1] Department of Chemical Sciences, Indian Institute of Science Education and Research Berhampur, Odisha, Berhampur
[2] Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Uttarakhand, Roorkee
[3] Department of Chemistry, Indian Institute of Technology Delhi, New Delhi
来源：
Biomolecular NMR Assignments | 2025年 / 19卷 / 1期
关键词：
IFN; IRF3; NMR resonance assignment; Transcription factor;
D O I：
10.1007/s12104-025-10234-5
中图分类号：
学科分类号：
摘要：
The Interferon Regulatory Factor (IRF) family of transcription factors is well known for its anti-viral activity in vertebrates. The IRF family comprises nine members (IRF1-9) which have the ability to induce the Interferon beta (IFNβ) promotor. The IRF3 and IRF7 are the key family members involved in the production of type I and type III IFN. IRF3 and IRF7 both comprise of a DNA binding domain (DBD) which binds to its cognate interferon responsive element (IRE) on its target gene promoters. Here, we report near complete backbone and partial side-chain resonance assignments of the DBD domain of the IRF3 subunit of the IRF family. The predicted secondary structure using the backbone chemical shifts largely conforms with that obtained from the crystal structure, with the TALOS-N predicted secondary structures showing slightly elongated β-strands. © The Author(s), under exclusive licence to Springer Nature B.V. 2025.
引用
收藏
页码：183 / 186
页数：3
相关论文
共 13 条
  • [1] Cheng C.S., Feldman K.E., Lee J., Verma S., Huang D.B., Huynh K., Chang M., Ponomarenko J.V., Sun S.C., Benedict C.A., Et al., The specificity of innate immune responses is enforced by repression of interferon response elements by NF-kappaB p50, Sci Signal, 4, (2011)
  • [2] De Ioannes P., Escalante C.R., Aggarwal A.K., Structures of Apo IRF-3 and IRF-7 DNA binding domains: effect of loop L1 on DNA binding, Nucleic Acids Res, 39, pp. 7300-7307, (2011)
  • [3] Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A., NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J Biomol NMR, 6, pp. 277-293, (1995)
  • [4] Honda K., Taniguchi T., IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors, Nat Rev Immunol, 6, pp. 644-658, (2006)
  • [5] Keller R.L.J., Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment, (2004)
  • [6] Kirshner J.R., Karpova A.Y., Kops M., Howley P.M., Identification of TRAIL as an interferon regulatory factor 3 transcriptional target, J Virol, 79, pp. 9320-9324, (2005)
  • [7] Krishnarjuna B., Jaipuria G., Thakur A., D'Silva P., Atreya H.S., Amino acid selective unlabeling for sequence specific resonance assignments in proteins, J Biomol NMR, 49, pp. 39-51, (2011)
  • [8] Kuroki S., Ando S., Ando I., Shoji A., Ozaki T., Webb G.A., Hydrogen-bonding effect on 15 N NMR chemical sifts of the glycine residue of oligopeptides in the solid state as studied by high-resolution solid-state Nmr spectroscopy, J Mol Struct, 240, (1990)
  • [9] Lin M.T., Sperling L.J., Schmidt F., Tang H.L., Samoilova M., Kumasaka R.I., Iwasaki T., Dikanov T., Rienstra S.A., Gennis R.B., A rapid and robust method for selective isotope labeling of proteins, Methods, 55, pp. 370-378, (2011)
  • [10] Panne D., Maniatis T., Harrison S.C., Crystal structure of ATF-2/c-Jun and IRF-3 bound to the interferon-beta enhancer, EMBO J, 23, pp. 4384-4393, (2004)
12