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Single particle cryo-EM dataset of the flexible and variable oligomeric state complex AP-1:Arf1:tetherin-HIV-Nef


ABSTRACT:

SUBMITTER: Kyle L Morris 

PROVIDER: EMPIAR-10176 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation.

Morris Kyle L KL   Buffalo Cosmo Z CZ   Stürzel Christina M CM   Heusinger Elena E   Kirchhoff Frank F   Ren Xuefeng X   Hurley James H JH  

Cell 20180701 3


The HIV accessory protein Nef counteracts immune defenses by subverting coated vesicle pathways. The 3.7 Å cryo-EM structure of a closed trimer of the clathrin adaptor AP-1, the small GTPase Arf1, HIV-1 Nef, and the cytosolic tail of the restriction factor tetherin suggested a mechanism for inactivating tetherin by Golgi retention. The 4.3 Å structure of a mutant Nef-induced dimer of AP-1 showed how the closed trimer is regulated by the dileucine loop of Nef. HDX-MS and mutational analysis were  ...[more]

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