Backbone and Ile-δ1, Leu, Val Methyl 1H, 13C and 15N NMR chemical shift assignments for human interferon- stimulated gene 15 protein

Cuifeng Yin, James M. Aramini, Li Chung Ma, John R. Cort, G. V.T. Swapna, Robert M. Krug, Gaetano T. Montelione

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Human interferon-stimulated gene 15 protein (ISG15), also called ubiquitin cross-reactive protein (UCRP), is the first identified ubiquitin-like protein containing two ubiquitin-like domains fused in tandem. The active form of ISG15 is conjugated to target proteins via the C-terminal glycine residue through an isopeptide bond in a manner similar to ubiquitin. The biological role of ISG15 is strongly associated with the modulation of cell immune function, and there is mounting evidence suggesting that many viral pathogens evade the host innate immune response by interfering with ISG15 conjugation to both host and viral proteins in a variety of ways. Here we report nearly complete backbone 1HN, 15N, 13C', and 13Cα, as well as side chain 13Cβ, methyl (Ile-δ1, Leu, Val), amide (Asn, Gln), and indole N-H (Trp) NMR resonance assignments for the 157-residue human ISG15 protein. These resonance assignments provide the basis for future structural and functional solution NMR studies of the biologically important human ISG15 protein.

Original languageEnglish (US)
Pages (from-to)215-219
Number of pages5
JournalBiomolecular NMR Assignments
Volume5
Issue number2
DOIs
StatePublished - Oct 2011

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Keywords

  • Backbone NMR resonance assignment
  • Human ISG15
  • Innate immune response
  • Ubiquitin-like protein

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