8D9S
AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated wide membrane tubes, centered on beta-Arf1
Summary for 8D9S
| Entry DOI | 10.2210/pdb8d9s/pdb |
| EMDB information | 27183 27190 |
| Descriptor | ADP ribosylation factor 1, Protein Nef, HLA class I histocompatibility antigen, A alpha chain, ... (9 entities in total) |
| Functional Keywords | trafficking, ap, hiv, viral protein-protein transport complex, viral protein/protein transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 60 |
| Total formula weight | 2142956.47 |
| Authors | Hooy, R.M.,Hurley, J.H. (deposition date: 2022-06-11, release date: 2022-11-09, Last modification date: 2024-06-12) |
| Primary citation | Hooy, R.M.,Iwamoto, Y.,Tudorica, D.A.,Ren, X.,Hurley, J.H. Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat. Sci Adv, 8:eadd3914-eadd3914, 2022 Cited by PubMed Abstract: The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to sequester major histocompatibility complex class I (MHC-I), evading immune detection. We found that AP-1:Arf1:Nef:MHC-I forms a coat on tubulated membranes without clathrin and determined its structure. The coat assembles via Arf1 dimer interfaces. AP-1-positive tubules are enriched in cells upon clathrin knockdown. Nef localizes preferentially to AP-1 tubules in cells, explaining how Nef sequesters MHC-I. Coat contact residues are conserved across Arf isoforms and the Arf-dependent AP complexes AP-1, AP-3, and AP-4. Thus, AP complexes can self-assemble with Arf1 into tubular coats without clathrin or other scaffolding factors. The AP-1:Arf1 coat defines the structural basis of a broader class of tubulovesicular membrane coats as an intermediate in clathrin vesicle formation from internal membranes and as an MHC-I sequestration mechanism in HIV-1 infection. PubMed: 36269825DOI: 10.1126/sciadv.add3914 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
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