title: Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein.
abstract: Agnoprotein is an important regulatory protein of the human polyoma JC virus (JCV) and plays critical roles during the viral replication cycle. It forms highly stable dimers and oligomers through its Leu/Ile/Phe-rich domain, which is important for the stability and function of the protein. We recently resolved the partial 3D structure of this protein by NMR using a synthetic peptide encompassing amino acids Thr17 to Gln52, where the Leu/Ile/Phe- rich region was found to adopt a major alpha-helix conformation spanning amino acids 23-39. Here, we report the resolution of the 3D structure of full-length JCV agnoprotein by NMR, which not only confirmed the existence of the previously reported major α-helix domain at the same position but also revealed the presence of an additional minor α-helix region spanning amino acid residues Leu6 to lys13. The remaining regions of the protein adopt an intrinsically unstructured conformation. J. Cell. Biochem. 118: 3268-3280, 2017. © 2017 Wiley Periodicals, Inc.
authors.affiliation: Université Paris Descartes, Sorbonne Paris Cité, Laboratoire de Cristallographie et RMN Biologiques, UMR 8015 CNRS, 4 av. de l'Observatoire, Paris, France.
authors.forename: Pascale
authors.initials: P
authors.lastname: Coric
authors.affiliation: Department of Neuroscience, Laboratory of Molecular Neurovirology, Lewis Katz School of Medicine at Temple University, 3500 N. Broad Street, Philadelphia, Pennsylvania, 19140.
authors.forename: A Sami
authors.initials: AS
authors.lastname: Saribas
authors.affiliation: Temple University School of Pharmacy, Moulder Center for Drug Discovery Research 3307 N. Broad Street, Philadelphia, Pennsylvania, 19140.
authors.forename: Magid
authors.initials: M
authors.lastname: Abou-Gharbia
authors.affiliation: Temple University School of Pharmacy, Moulder Center for Drug Discovery Research 3307 N. Broad Street, Philadelphia, Pennsylvania, 19140.
authors.forename: Wayne
authors.initials: W
authors.lastname: Childers
authors.affiliation: Temple University School of Pharmacy, Moulder Center for Drug Discovery Research 3307 N. Broad Street, Philadelphia, Pennsylvania, 19140.
authors.forename: Jon H
authors.initials: JH
authors.lastname: Condra
authors.affiliation: Department of Neuroscience, Laboratory of Molecular Neurovirology, Lewis Katz School of Medicine at Temple University, 3500 N. Broad Street, Philadelphia, Pennsylvania, 19140.
authors.forename: Martyn K
authors.initials: MK
authors.lastname: White
authors.affiliation: Department of Neuroscience, Laboratory of Molecular Neurovirology, Lewis Katz School of Medicine at Temple University, 3500 N. Broad Street, Philadelphia, Pennsylvania, 19140.
authors.forename: Mahmut
authors.identifier: 0000-0003-2452-3810
authors.initials: M
authors.lastname: Safak
authors.affiliation: Université Paris Descartes, Sorbonne Paris Cité, Laboratoire de Cristallographie et RMN Biologiques, UMR 8015 CNRS, 4 av. de l'Observatoire, Paris, France.
authors.forename: Serge
authors.initials: S
authors.lastname: Bouaziz
mesh_terms: D006801:Humans; D007577:JC Virus / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D054334:Viral Regulatory and Accessory Proteins / Q000737:chemistry*; D000086082:Viroporin Proteins
chemical_list: D054334:Viral Regulatory and Accessory Proteins; C042559:agnoprotein, polyomavirus; D000086082:Viroporin Proteins
keywords: AGNOPROTEIN; ALPHA-HELIX; BKV; DIMER; DNA; INTRINSICALLY UNSTRUCTURED; JCV; MERKEL CELL; NMR; OLIGOMER; POLYOMAVIRUS; PROGRESSIVE MULTIFOCAL LEUKOENCEPHALOPATHY; REPLICATION; SV40