Backbone assignment of the N-terminal polyomavirus large T antigen

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

doi:10.1007/s12104-009-9155-7

Backbone assignment of the N-terminal polyomavirus large T antigen

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

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Chemie und Metabolomics

13 Zitate (Scopus)

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.

Originalsprache	Englisch
Zeitschrift	Biomolecular NMR Assignments
Jahrgang	3
Ausgabenummer	1
Seiten (von - bis)	119-123
Seitenumfang	5
ISSN	1874-2718
DOIs	https://doi.org/10.1007/s12104-009-9155-7
Publikationsstatus	Veröffentlicht - 06.2009

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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.

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title = "Backbone assignment of the N-terminal polyomavirus large T antigen",

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.",

author = "Konstantin Knoblich and Sara Whittaker and Christian Ludwig and Paul Michiels and Tao Jiang and Brian Schaffhausen and Ulrich G{\"u}nther",

note = "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.",

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month = jun,

doi = "10.1007/s12104-009-9155-7",

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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.

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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.

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Backbone assignment of the N-terminal polyomavirus large T antigen

Abstract

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