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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-10177 | biostudies-other |

REPOSITORIES: biostudies-other

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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]

PMID: 30053425

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