Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef.

@article{Geyer2001DomainAS,
  title={Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef.},
  author={Matthias Geyer and Boris Matija Peterlin},
  journal={FEBS letters},
  year={2001},
  volume={496 2-3},
  pages={91-5}
}
The accessory Nef protein from human and simian immunodeficiency viruses is critical for efficient viral replication and pathogenesis. Here we present an assembly of the full length structure of HIV-1 Nef, allele NL4-3, based on the previously solved anchor and core domain structures. The center part of the 33 residue encompassing flexible loop at the C-terminus of Nef, involved in Nef internalization and CD4 endocytosis, has been modelled. The degree of sequence conservation in HIV-1 Nef… CONTINUE READING

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