2mj2
From Proteopedia
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| - | + | {{STRUCTURE_2mj2| PDB=2mj2 | SCENE= }} | |
| + | ===Structure of the dimerization domain of the human polyoma, JC virus agnoprotein is an amphipathic alpha-helix.=== | ||
| + | {{ABSTRACT_PUBMED_23747198}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/AGNO_POVJC 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.<ref>PMID:11517407</ref> <ref>PMID:12165856</ref> <ref>PMID:20300659</ref> | ||
| - | + | ==About this Structure== | |
| + | [[2mj2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJ2 OCA]. | ||
| - | + | ==Reference== | |
| + | <ref group="xtra">PMID:023747198</ref><references group="xtra"/><references/> | ||
| + | [[Category: Abou-Gharbia, M.]] | ||
| + | [[Category: Bouaziz, S.]] | ||
| + | [[Category: Childers, W.]] | ||
| + | [[Category: Coric, P.]] | ||
| + | [[Category: Safak, M.]] | ||
| + | [[Category: Saribas, S A.]] | ||
| + | [[Category: White, M.]] | ||
| + | [[Category: Agnoprotein]] | ||
| + | [[Category: Dna replication]] | ||
| + | [[Category: Polyomavirus jcv]] | ||
| + | [[Category: Progressive multifocal leukoencephalopathy]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 07:42, 23 April 2014
Contents |
Structure of the dimerization domain of the human polyoma, JC virus agnoprotein is an amphipathic alpha-helix.
Template:ABSTRACT PUBMED 23747198
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]
About this Structure
2mj2 is a 1 chain structure. Full experimental information is available from OCA.
Reference
- Sami Saribas A, Abou-Gharbia M, Childers W, Sariyer IK, White MK, Safak M. Essential roles of Leu/Ile/Phe-rich domain of JC virus agnoprotein in dimer/oligomer formation, protein stability and splicing of viral transcripts. Virology. 2013 Aug 15;443(1):161-76. doi: 10.1016/j.virol.2013.05.003. Epub 2013 , Jun 6. PMID:23747198 doi:http://dx.doi.org/10.1016/j.virol.2013.05.003
- ↑ 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
- ↑ 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
- ↑ 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
