7URT
T=1 particle HIV-1 CA G60A/G61P/M66A
Summary for 7URT
| Entry DOI | 10.2210/pdb7urt/pdb |
| EMDB information | 26718 |
| Descriptor | Gag polyprotein, INOSITOL HEXAKISPHOSPHATE (2 entities in total) |
| Functional Keywords | hiv-1, capsid, declination, pentamer, hexamer, virus like particle |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 26944.47 |
| Authors | Pornillos, O.,Ganser-Pornillos, B.K.,Schirra, R.T. (deposition date: 2022-04-22, release date: 2023-02-15, Last modification date: 2024-06-12) |
| Primary citation | Schirra, R.T.,Dos Santos, N.F.B.,Zadrozny, K.K.,Kucharska, I.,Ganser-Pornillos, B.K.,Pornillos, O. A molecular switch modulates assembly and host factor binding of the HIV-1 capsid. Nat.Struct.Mol.Biol., 30:383-390, 2023 Cited by PubMed Abstract: The HIV-1 capsid is a fullerene cone made of quasi-equivalent hexamers and pentamers of the viral CA protein. Typically, quasi-equivalent assembly of viral capsid subunits is controlled by a molecular switch. Here, we identify a Thr-Val-Gly-Gly motif that modulates CA hexamer/pentamer switching by folding into a 3 helix in the pentamer and random coil in the hexamer. Manipulating the coil/helix configuration of the motif allowed us to control pentamer and hexamer formation in a predictable manner, thus proving its function as a molecular switch. Importantly, the switch also remodels the common binding site for host factors that are critical for viral replication and the new ultra-potent HIV-1 inhibitor lenacapavir. This study reveals that a critical assembly element also modulates the post-assembly and viral replication functions of the HIV-1 capsid and provides new insights on capsid function and inhibition. PubMed: 36759579DOI: 10.1038/s41594-022-00913-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.39 Å) |
Structure validation
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