TY - JOUR
T1 - Backbone assignment of the N-terminal polyomavirus large T antigen
AU - Knoblich, Konstantin
AU - Whittaker, Sara
AU - Ludwig, Christian
AU - Michiels, Paul
AU - Jiang, Tao
AU - Schaffhausen, Brian
AU - Günther, Ulrich
N1 - Funding Information:
Acknowledgments We would like to thank Michael Overduin and Tim Knowles for helpful discussions. KK is supported by a Cancer Research UK studentship. BS is supported by the National Institute of Health (34722 to BSS). Protonless 13C-observed spectra were obtained at the CERM NMR facility supported by the EU-NMR program (RII3-026145). We thank Isabella Felli for essential advice in choosing optimal pulse sequences.
Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2009/6
Y1 - 2009/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=67349183679&partnerID=8YFLogxK
U2 - 10.1007/s12104-009-9155-7
DO - 10.1007/s12104-009-9155-7
M3 - Journal articles
C2 - 19636961
AN - SCOPUS:67349183679
SN - 1874-2718
VL - 3
SP - 119
EP - 123
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
IS - 1
ER -
