7urt

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T=1 particle HIV-1 CA G60A/G61P/M66AT=1 particle HIV-1 CA G60A/G61P/M66A

Structural highlights

7urt is a 1 chain structure with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.39Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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(10) 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.

A molecular switch modulates assembly and host factor binding of the HIV-1 capsid.,Schirra RT, Dos Santos NFB, Zadrozny KK, Kucharska I, Ganser-Pornillos BK, Pornillos O Nat Struct Mol Biol. 2023 Mar;30(3):383-390. doi: 10.1038/s41594-022-00913-5. , Epub 2023 Feb 9. PMID:36759579[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Schirra RT, Dos Santos NFB, Zadrozny KK, Kucharska I, Ganser-Pornillos BK, Pornillos O. A molecular switch modulates assembly and host factor binding of the HIV-1 capsid. Nat Struct Mol Biol. 2023 Mar;30(3):383-390. PMID:36759579 doi:10.1038/s41594-022-00913-5

7urt, resolution 2.39Å

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OCA