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@ARTICLE{Venkatachari:13094,
      author       = {Venkatachari, N.J. and Walker, L.A. and Tastan, O. and Le,
                      T. and Dempsey, T.M. and Li, Y. and Yanamala, N. and
                      Srinivasan, A. and Klein-Seetharaman, J. and Montelaro, R.C.
                      and Ayyavoo, V.},
      title        = {{H}uman immunodeficiency virus type 1 {V}pr:
                      {O}ligomerization is an essential feature for its
                      incorporation into virus particles},
      journal      = {Virology},
      volume       = {7},
      issn         = {0042-6822},
      address      = {San Diego, Calif. [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-13094},
      pages        = {119},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {HIV-1 Vpr, a nonstructural viral protein associated with
                      virus particles, has a positive role in the efficient
                      transport of PIC into the nucleus of non-dividing target
                      cells and enhances virus replication in primary T cells. Vpr
                      is a 96 amino acid protein and the structure by NMR shows
                      three helical domains. Vpr has been shown to exist as dimers
                      and higher order oligomers. Considering the multifunctional
                      nature of Vpr, the contribution of distinct helical domains
                      to the dimer/oligomer structure of Vpr and the relevance of
                      this feature to its functions are not clear. To address
                      this, we have utilized molecular modeling approaches to
                      identify putative models of oligomerization. The predicted
                      interface residues were subjected to site-directed
                      mutagenesis and evaluated their role in intermolecular
                      interaction and virion incorporation. The interaction
                      between Vpr molecules was monitored by Bimolecular
                      Fluorescence complementation (BiFC) method. The results show
                      that Vpr forms oligomers in live cells and residues in
                      helical domains play critical roles in oligomerization.
                      Interestingly, Vpr molecules defective in oligomerization
                      also fail to incorporate into the virus particles. Based on
                      the data, we suggest that oligomerization of Vpr is
                      essential for virion incorporation property and may also
                      have a role in the events associated with virus infection.},
      keywords     = {Amino Acid Sequence / Cell Line / HIV-1: chemistry / HIV-1:
                      genetics / HIV-1: metabolism / Humans / Molecular
                      Conformation / Molecular Sequence Data / Protein Structure,
                      Tertiary / Sequence Alignment / Virion: chemistry / Virion:
                      genetics / Virion: metabolism / vpr Gene Products, Human
                      Immunodeficiency Virus: chemistry / vpr Gene Products, Human
                      Immunodeficiency Virus: genetics / vpr Gene Products, Human
                      Immunodeficiency Virus: metabolism / vpr Gene Products,
                      Human Immunodeficiency Virus (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Virology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20529298},
      pmc          = {pmc:PMC2894018},
      UT           = {WOS:000244272500011},
      doi          = {10.1186/1743-422X-7-119},
      url          = {https://juser.fz-juelich.de/record/13094},
}