8TY6
Disulfide-stabilized HIV-1 CA hexamer in complex with PQBP1 Nt
Summary for 8TY6
| Entry DOI | 10.2210/pdb8ty6/pdb |
| EMDB information | 41711 |
| Descriptor | Capsid protein p24 (1 entity in total) |
| Functional Keywords | capsid, innate immune sensor, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 6 |
| Total formula weight | 152767.63 |
| Authors | Piacentini, J.,Pornillos, O.,Ganser-Pornillos, B.K. (deposition date: 2023-08-24, release date: 2024-03-06, Last modification date: 2024-11-06) |
| Primary citation | Piacentini, J.,Allen, D.S.,Ganser-Pornillos, B.K.,Chanda, S.K.,Yoh, S.M.,Pornillos, O. Molecular Determinants of PQBP1 Binding to the HIV-1 Capsid Lattice. J.Mol.Biol., 436:168409-168409, 2024 Cited by PubMed Abstract: Human immunodeficiency virus type 1 (HIV-1) stimulates innate immune responses upon infection, including cyclic GMP-AMP synthase (cGAS) signaling that results in type I interferon production. HIV-1-induced activation of cGAS requires the host cell factor polyglutamine binding protein 1 (PQBP1), an intrinsically disordered protein that bridges capsid recognition and cGAS recruitment. However, the molecular details of PQBP1 interactions with the HIV-1 capsid and their functional implications remain poorly understood. Here, we show that PQBP1 binds to HIV-1 capsids through charge complementing contacts between acidic residues in the N-terminal region of PQBP1 and an arginine ring in the central channel of the HIV-1 CA hexamer that makes up the viral capsid. These studies reveal the molecular details of PQBP1's primary interaction with the HIV-1 capsid and suggest that additional elements are likely to contribute to stable capsid binding. PubMed: 38128824DOI: 10.1016/j.jmb.2023.168409 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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