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J Cell Physiol. 2016 Oct;231(10):2115-27. doi: 10.1002/jcp.25329. Epub 2016 Feb 24.

Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses.

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Department of Neuroscience, Laboratory of Molecular Neurovirology, MERB-757, Temple University Lewis Katz School of Medicine, Philadelphia, Pennsylvania.
Université Paris Descartes, Sorbonne Paris Cité, Laboratoire de Cristallographie et RMN Biologiques, 4 av. de l'Observatoire, Paris, France.
Moulder Center for Drug Discovery Research, Temple University School of Pharmacy, Philadelphia, Pennsylvania.


Agnoprotein is an important regulatory protein of polyomaviruses, including JCV, BKV, and SV40. In the absence of its expression, these viruses are unable to sustain their productive life cycle. It is a highly basic phosphoprotein that localizes mostly to the perinuclear area of infected cells, although a small amount of the protein is also found in nucleus. Much has been learned about the structure and function of this important regulatory protein in recent years. It forms highly stable dimers/oligomers in vitro and in vivo through its Leu/Ile/Phe-rich domain. Structural NMR studies revealed that this domain adopts an alpha-helix conformation and plays a critical role in the stability of the protein. It associates with cellular proteins, including YB-1, p53, Ku70, FEZ1, HP1α, PP2A, AP-3, PCNA, and α-SNAP; and viral proteins, including small t antigen, large T antigen, HIV-1 Tat, and JCV VP1; and significantly contributes the viral transcription and replication. This review summarizes the recent advances in the structural and functional properties of this important regulatory protein. J. Cell. Physiol. 231: 2115-2127, 2016.

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