Backbone assignment of the N-terminal polyomavirus large T antigen View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-04-09

AUTHORS

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

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. More... »

PAGES

119-123

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12104-009-9155-7

DOI

http://dx.doi.org/10.1007/s12104-009-9155-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046595941

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19636961


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