5nhq

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Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus AgnoproteinNuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein

Structural highlights

5nhq is a 1 chain structure with sequence from JC polyomavirus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AGNO_POVJC Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins.[1] [2] [3]

Publication Abstract from PubMed

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 domain was found to adopt a major alpha-helix conformation spanning amino acids 23 to 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 alpha-helix domain at the same position but also revealed the presence of an additional minor alpha-helix region spanning amino acid residues Leu6 to Ala10. The remaining regions of the protein adopt an intrinsically unstructured conformation. This article is protected by copyright. All rights reserved.

Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein.,Coric P, Saribas AS, Abou-Gharbia M, Childers W, Condra J, White MK, Safak M, Bouaziz S J Cell Biochem. 2017 Mar 10. doi: 10.1002/jcb.25977. PMID:28295503[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Okada Y, Endo S, Takahashi H, Sawa H, Umemura T, Nagashima K. Distribution and function of JCV agnoprotein. J Neurovirol. 2001 Aug;7(4):302-6. PMID:11517407
  2. ↑ Darbinyan A, Darbinian N, Safak M, Radhakrishnan S, Giordano A, Khalili K. Evidence for dysregulation of cell cycle by human polyomavirus, JCV, late auxiliary protein. Oncogene. 2002 Aug 15;21(36):5574-81. PMID:12165856 doi:http://dx.doi.org/10.1038/sj.onc.1205744
  3. ↑ Suzuki T, Orba Y, Okada Y, Sunden Y, Kimura T, Tanaka S, Nagashima K, Hall WW, Sawa H. The human polyoma JC virus agnoprotein acts as a viroporin. PLoS Pathog. 2010 Mar 12;6(3):e1000801. doi: 10.1371/journal.ppat.1000801. PMID:20300659 doi:http://dx.doi.org/10.1371/journal.ppat.1000801
  4. ↑ Coric P, Saribas AS, Abou-Gharbia M, Childers W, Condra J, White MK, Safak M, Bouaziz S. Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein. J Cell Biochem. 2017 Mar 10. doi: 10.1002/jcb.25977. PMID:28295503 doi:http://dx.doi.org/10.1002/jcb.25977
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