Backbone assignment of the N-terminal polyomavirus large T antigen

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

*Corresponding author for this work
12 Citations (Scopus)


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
JournalBiomolecular NMR Assignments
Issue number1
Pages (from-to)119-123
Number of pages5
Publication statusPublished - 06.2009

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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