Active site remodeling switches HIV specificity of antiretroviral TRIMCyp

@article{Price2009ActiveSR,
  title={Active site remodeling switches HIV specificity of antiretroviral TRIMCyp},
  author={Amanda J. Price and Flavia Marzetta and Michael Lammers and Laura M. J. Ylinen and Torsten Schaller and Sam John Wilson and Greg J. Towers and Leo C James},
  journal={Nature Structural &Molecular Biology},
  year={2009},
  volume={16},
  pages={1036-1042}
}
TRIMCyps are primate antiretroviral proteins that potently inhibit HIV replication. Here we describe how rhesus macaque TRIMCyp (RhTC) has evolved to target and restrict HIV-2. We show that the ancestral cyclophilin A (CypA) domain of RhTC targets HIV-2 capsid with weak affinity, which is strongly increased in RhTC by two mutations (D66N and R69H) at the expense of HIV-1 binding. These mutations disrupt a constraining intramolecular interaction in CypA, triggering the complete restructuring… CONTINUE READING
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