Dynamic allostery governs cyclophilin A–HIV capsid interplay

@article{Lu2015DynamicAG,
  title={Dynamic allostery governs cyclophilin A–HIV capsid interplay},
  author={Manman Lu and Guangjin Hou and Hui-lan Zhang and Christopher L. Suiter and J. Ahn and I. Byeon and J. R. Perilla and C. Langmead and I. Hung and P. Gor’kov and Z. Gan and W. Brey and C. Aiken and P. Zhang and K. Schulten and A. Gronenborn and T. Polenova},
  journal={Proceedings of the National Academy of Sciences},
  year={2015},
  volume={112},
  pages={14617 - 14622}
}
  • Manman Lu, Guangjin Hou, +14 authors T. Polenova
  • Published 2015
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences
  • Significance The mechanisms of how Cyclophilin A (CypA) regulates HIV-1 infectivity remain poorly understood. We examined the role of dynamics in capsid (CA) protein assemblies by magic-angle-spinning NMR. The assembled CA is highly dynamic. Dipolar tensors calculated from molecular dynamics trajectories are in quantitative agreement with the NMR results. Motions in the CypA loop are sequence-dependent and attenuated in the escape mutants A92E and G94D. Dynamics are similar in escape mutants… CONTINUE READING
    Quenching protein dynamics interferes with HIV capsid maturation
    • 27
    • Open Access
    Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A
    • 3
    • Open Access
    Molecular Architecture of the Retroviral Capsid.
    • 30
    • Open Access
    Capsid-Dependent Host Factors in HIV-1 Infection.
    • 46
    • Open Access

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 43 REFERENCES
    Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors
    • 377
    Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A
    • 199
    • Open Access
    Target Cell Type-Dependent Modulation of Human Immunodeficiency Virus Type 1 Capsid Disassembly by Cyclophilin A
    • 101
    • Open Access
    HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358
    • 64
    • Open Access
    Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function
    • 202
    • Open Access
    The Host Proteins Transportin SR2/TNPO3 and Cyclophilin A Exert Opposing Effects on HIV-1 Uncoating
    • 104
    • Open Access