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Biomol NMR Assign. 2009 Jun;3(1):119-23. doi: 10.1007/s12104-009-9155-7. Epub 2009 Apr 9.

Backbone assignment of the N-terminal polyomavirus large T antigen.

Author information

1
HWB-NMR, School for Cancer Sciences, Birmingham University, Birmingham, B15 2TT, UK.

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 (1)H, (15)N, (13)C backbone and (13)C 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.

PMID:
19636961
DOI:
10.1007/s12104-009-9155-7
[Indexed for MEDLINE]

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