Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.

@article{Liu2016CyclophilinAS,
  title={Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.},
  author={Chuang Liu and Juan R. Perilla and Jiying Ning and Manman Lu and Guangjin Hou and Ruben Ramalho and Benjamin A Himes and Gongpu Zhao and Gregory J. Bedwell and In-Ja L. Byeon and Jinwoo Ahn and Angela M. Gronenborn and Peter E. Prevelige and Itay Rousso and Christopher Aiken and Tatyana Polenova and Klaus Schulten and Peijun Zhang},
  journal={Nature communications},
  year={2016},
  volume={7},
  pages={10714}
}
The host cell factor cyclophilin A (CypA) interacts directly with the HIV-1 capsid and regulates viral infectivity. Although the crystal structure of CypA in complex with the N-terminal domain of the HIV-1 capsid protein (CA) has been known for nearly two decades, how CypA interacts with the viral capsid and modulates HIV-1 infectivity remains unclear. We determined the cryoEM structure of CypA in complex with the assembled HIV-1 capsid at 8-Å resolution. The structure exhibits a distinct CypA… CONTINUE READING
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