2mj2 | pdb_00002mj2

Structure of the dimerization domain of the human polyoma, JC virus agnoprotein is an amphipathic alpha-helix.

spinqualitylabelsall models 2mj2, 17 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mj2 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. 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. Publication Abstract from PubMed Agnoprotein is one of the key regulatory proteins of polyomaviruses, including JCV, BKV and SV40 and is required for a productive viral life cycle. We have recently reported that agnoprotein forms stable dimer/oligomers mediated by a predicted amphipathic alpha-helix, spanning amino acids (aa), 17 to 42. Deletion of the alpha-helix renders a replication incompetent virus. Here, we have further characterized this region by a systematic deletion and substitution mutagenesis and demonstrated that a Leu/Ile/Phe-rich domain, (spanning aa 28-39) within alpha-helix is indispensable for agnoprotein structure and function. Deletion of aa 30-37 severely affects the dimer/oligomer formation and stable expression of the protein. Mutagenesis data also indicate that the residues, 34-36, may be involved in regulation of the splicing events of JCV transcripts. Collectively, these data suggest that the Leu/Ile/Phe-rich domain plays critical roles in agnoprotein function and thus represents a potential target for developing novel therapeutics against JCV infections. Essential roles of Leu/Ile/Phe-rich domain of JC virus agnoprotein in dimer/oligomer formation, protein stability and splicing of viral transcripts.,Sami Saribas A, Abou-Gharbia M, Childers W, Sariyer IK, White MK, Safak M Virology. 2013 Aug 15;443(1):161-76. doi: 10.1016/j.virol.2013.05.003. Epub 2013 , Jun 6. PMID:23747198 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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