6ES8
HIV capsid hexamer with IP6 ligand
Summary for 6ES8
| Entry DOI | 10.2210/pdb6es8/pdb |
| Descriptor | Gag protein, INOSITOL HEXAKISPHOSPHATE (3 entities in total) |
| Functional Keywords | hiv, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 25164.21 |
| Authors | James, L.C. (deposition date: 2017-10-19, release date: 2018-08-15, Last modification date: 2024-01-17) |
| Primary citation | Mallery, D.L.,Marquez, C.L.,McEwan, W.A.,Dickson, C.F.,Jacques, D.A.,Anandapadamanaban, M.,Bichel, K.,Towers, G.J.,Saiardi, A.,Bocking, T.,James, L.C. IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis. Elife, 7:-, 2018 Cited by PubMed Abstract: The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP, transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate inside the capsid. An arginine ring within the pore coordinates IP, which strengthens capsid hexamers by almost 10°C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. Moreover, encapsidated reverse transcription assays reveal that, once stabilised by IP, the accumulation of new viral DNA inside the capsid increases >100 fold. Remarkably, isotopic labelling of inositol in virus-producing cells reveals that HIV selectively packages over 300 IP molecules per infectious virion. We propose that HIV recruits IP to regulate capsid stability and uncoating, analogous to picornavirus pocket factors. HIV-1/IP/capsid/co-factor/reverse transcription. PubMed: 29848441DOI: 10.7554/eLife.35335 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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