Fig. 1 | Nature Communications

Fig. 1

From: Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer

Fig. 1

Molecular architecture and comparison of the soluble, cleavage-independent BG505 NFL.664 with natively cleaved designs. a The crystal asymmetric unit of the complex comprises one copy of the BG505 NFL.664 protomer (salmon) bound to one PGT122 Fab (LC: gray, HC: wheat) at the N332 site and PGV19 (LC: cyan, HC: yellow) at the CD4bs. Inset: The gp41 tryptophan clasps (green) are still present on the vertices of the NFL trimer’s lower aperture. The bottom panel schematic illustrates the cleavage dependence and design variations between different trimeric Env constructs16, 20, 37. b Comparison of the crystal structures of BG505 NFL.664 and BG505 SOSIP (PDB 5CEZ, gray) (side view of protomer and top view of trimer). c Comparison of the crystal structure of BG505 NFL.664 and the cryo-EM structure of JRFL WTΔCT (PDB 5FUU, dark blue) (side view of protomer and top view of trimer). The large RMSD between the compared trimer structures arises from the asymmetry in the JRFL WTΔCT induced by binding of two PGT151 antibodies per trimer

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