6VHI

Crystal structure of the human ILRUN Fw domain

Summary for 6VHI

• Entry DOI: 10.2210/pdb6vhi/pdb
• Descriptor: Protein ILRUN (2 entities in total)
• Functional Keywords: fw domain, innate immune system, immunoglobulin fold, immune system
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 13384.15

Authors

Caputo, A.T.,Adams, T.E. (deposition date: 2020-01-09, release date: 2020-07-01, Last modification date: 2023-10-11)

Primary citation

Ambrose, R.L.,Brice, A.M.,Caputo, A.T.,Alexander, M.R.,Tribolet, L.,Liu, Y.C.,Adams, T.E.,Bean, A.G.D.,Stewart, C.R.
Molecular characterisation of ILRUN, a novel inhibitor of proinflammatory and antimicrobial cytokines.
Heliyon, 6:e04115-e04115, 2020

PubMed Abstract: Regulation of type-I interferon (IFN) production is essential to the balance between antimicrobial defence and autoimmune disorders. The human protein-coding gene ILRUN (inflammation and lipid regulator with UBA-like and NBR1-like domains, previously C6orf106) was recently characterised as an inhibitor of antiviral and proinflammatory cytokine (interferon-alpha/beta and tumor necrosis factor alpha) transcription. Currently there is a paucity of information about the molecular characteristics of ILRUN, despite it being associated with several diseases including virus infection, coronary artery disease, obesity and cancer. Here, we characterise ILRUN as a highly phylogenetically conserved protein containing UBA-like and a NBR1-like domains that are both essential for inhibition of type-I interferon and tumor necrosis factor alpha) transcription in human cells. We also solved the crystal structure of the NBR1-like domain, providing insights into its potential role in ILRUN function. This study provides critical information for future investigations into the role of ILRUN in health and disease.

PubMed: 32518853
DOI: 10.1016/j.heliyon.2020.e04115

Experimental method

X-RAY DIFFRACTION (2.46 Å)