Skip to main content
Advertisement

< Back to Article

A high-affinity RBD-targeting nanobody improves fusion partner’s potency against SARS-CoV-2

Fig 2

Crystal structure of the SR31-RBD complex.

(A) The overall structure of SR31 (light blue) in complex with RBD (grey) which contains Asn343-linked glycans (cyan). The expanded view highlights a deep hydrophobic pocket (green) for CDR3 binding. (B) The overall structure viewed at a different angle. (C) 2Fo-Fc map of the Asn343-linked glycans. MAN, mannose; BMA, β-D-mannose; FUC, fucose; NAG, N-acetylglucosamine. (D-G) Detailed interactions between RBD and the CDR1 (D), CDR2 (E), and CDR3 (F, G). The hydrophobic network formed between CDR3 (orange) and the hydrophobic pocket in RBD (grey) is shown in G. Residues from SR31 are labeled with black texts and residues from RBD are labeled with grey texts. Dash lines indicate hydrogen bonds or salt bridges within 3.6 Å.

Fig 2

doi: https://doi.org/10.1371/journal.ppat.1009328.g002