Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation.
Journal, issue, pages	Cell, Vol. 174, Issue 3, Page 659-671.e14, Year 2018
Publish date	Jul 26, 2018
Authors	Kyle L Morris / Cosmo Z Buffalo / Christina M Stürzel / Elena Heusinger / Frank Kirchhoff / Xuefeng Ren / James H Hurley /
PubMed Abstract	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, ...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 used to show how cargo dynamics leads to alternative Arf1 trimerization, directing Nef targets to be either retained at the trans-Golgi or sorted to lysosomes. Phosphorylation of the NL4-3 M-Nef was shown to regulate AP-1 trimerization, explaining how O-Nefs lacking this phosphosite counteract tetherin but most M-Nefs do not. These observations show how the higher-order organization of a vesicular coat can be allosterically modulated to direct cargoes to distinct fates.
External links	Cell / PubMed:30053425 / PubMed Central
Methods	EM (single particle)
Resolution	3.73 - 6.8 Å
Structure data	7453 6d83 EMDB-7453: Structure of the HIV-Nef dileucine mutant bound AP-1:Arf1 dimer monomeric subunit PDB-6d83: Structure of the cargo bound AP-1:Arf1:tetherin-Nef (L164A, L165A) dileucine mutant dimer monomeric subunit Method: EM (single particle) / Resolution: 4.27 Å 7454 6d84 EMDB-7454: Structure of the HIV-Nef dileucine mutant bound AP-1:Arf1 dimer PDB-6d84: Structure of the cargo bound AP-1:Arf1:tetherin-Nef (L164A, L165A) dileucine mutant dimer Method: EM (single particle) / Resolution: 6.72 Å 7455 6dff EMDB-7455, PDB-6dff: Structure of the cargo bound AP-1:Arf1:tetherin-Nef monomer Method: EM (single particle) / Resolution: 3.9 Å EMDB-7456: Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer monomeric subunit after focussed classification Method: EM (single particle) / Resolution: 4.05 Å 7457 6cm9 EMDB-7457: Structure of the HIV-Nef bound AP-1:Arf1 closed trimer monomeric subunit PDB-6cm9: Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer monomeric subunit Method: EM (single particle) / Resolution: 3.73 Å EMDB-7458: Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer Method: EM (single particle) / Resolution: 4.27 Å 7563 6cri EMDB-7563: Structure of the HIV-Nef tetherin cargo bound AP-1:Arf1 stable closed trimer PDB-6cri: Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer Method: EM (single particle) / Resolution: 6.8 Å
Chemicals	ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM / Guanosine triphosphate ChemComp-MG*: Unknown entry
Source	homo sapiens (human) human immunodeficiency virus 1 mus musculus (house mouse)
Keywords	VIRAL PROTEIN / PROTEIN TRANSPORT / AP / HIV / Nef / trafficking / TRANSPORT PROTEIN