Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity.

@article{Auclair2007MassSA,
  title={Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity.},
  author={Jared R Auclair and Karin M. Green and Shivender M. D. Shandilya and James Erwin Evans and Mohan Somasundaran and Celia A Schiffer},
  journal={Proteins},
  year={2007},
  volume={69 2},
  pages={
          270-84
        }
}
HIV-1 Vif, an accessory protein in the viral genome, performs an important role in viral pathogenesis by facilitating the degradation of APOBEC3G, an endogenous cellular inhibitor of HIV-1 replication. In this study, intrinsically disordered regions are predicted in HIV-1 Vif using sequence-based algorithms. Intrinsic disorder may explain why traditional structure determination of HIV-1 Vif has been elusive, making structure-based drug design impossible. To characterize HIV-1 Vif's structural… CONTINUE READING

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