Backbone assignment of the N-terminal polyomavirus large T antigen
Research output: Contribution to journal › Article › peer-review
Authors
Colleges, School and Institutes
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.
Details
Original language | English |
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Pages (from-to) | 119-123 |
Number of pages | 5 |
Journal | Biomolecular NMR Assignments |
Volume | 3 |
Issue number | 1 |
Publication status | Published - 1 Jun 2009 |
Keywords
- Retinoblastoma protein, Polyomavirus, Natively unfolded proteins, NMR assignments, Large T antigen