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Title | Molecular Determinants of PQBP1 Binding to the HIV-1 Capsid Lattice. |
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Journal, issue, pages | J Mol Biol, Vol. 436, Issue 4, Page 168409, Year 2024 |
Publish date | Feb 15, 2024 |
Authors | Juliana Piacentini / Dale S Allen / Barbie K Ganser-Pornillos / Sumit K Chanda / Sunnie M Yoh / Owen Pornillos / |
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- ...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. |
External links | J Mol Biol / PubMed:38128824 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 Å |
Structure data | EMDB-41711, PDB-8ty6: |
Source |
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Keywords | VIRAL PROTEIN / capsid / innate immune sensor |