Backbone assignment of the N-terminal polyomavirus large T antigen

Konstantin Knoblich, Sara Whittaker, Christian Ludwig, Paul Michiels, Tao Jiang, Brian Schaffhausen, Ulrich Günther

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12 Citations (Scopus)

Abstract

Polyoma Large T antigen (PyLT) is a viral oncoprotein that targets cell proteins important for growth regulation. PyLT has two functional domains. Here we report 1H, 15N, 13C backbone and 13C beta assignments of 76% of the residues of the polyomavirus large T antigen N-terminal domain (PyLTNT) that is sufficient to regulate cell phenotype. PyLTNT is substantially unfolded even in regions known to be critical for its biological function. The protein also includes a previously characterised J domain that although conformationally influenced by the residue extension, retains its folded state unlike the majority of the protein sequence.

Original languageEnglish
Pages (from-to)119-123
Number of pages5
JournalBiomolecular NMR Assignments
Volume3
Issue number1
DOIs
Publication statusPublished - Jun 2009
Externally publishedYes

Keywords

  • Large T antigen
  • Natively unfolded proteins
  • NMR assignments
  • Polyomavirus
  • Retinoblastoma protein

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