Backbone assignment of the N-terminal polyomavirus large T antigen.
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.
Knoblich
Konstantin
K
HWB-NMR, School for Cancer Sciences, Birmingham University, Birmingham, B15 2TT, UK.
Whittaker
Sara
S
Ludwig
Christian
C
Michiels
Paul
P
Jiang
Tao
T
Schaffhausen
Brian
B
Günther
Ulrich
U
D000595:Amino Acid Sequence; D000957:Antigens, Viral, Tumor / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D011120:Polyomavirus / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D000957:Antigens, Viral, Tumor; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons