Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization
Fig 5
Nano-32 in complex with the GII.10 domain.
The X-ray crystal structure of the GII.10 domain Nano-32 complex was determined to 2.1Å resolution. The asymmetric unit cell contained one P domain dimer and two Nanobodies in space group P41212. The interface with the surface area of 650 Å2 was considered biologically relevant. (A) The complex was colored according to Fig 3 with Nano-32 (yellow). (B) The Nano-32 bound to the side of the P1 subdomain in the cleft between two monomers. (C) A close-up view of GII.10 P domain and Nano-32 interacting residues. The P domain hydrogen bond interactions included side chain and main chain interactions from both monomers. Direct hydrogen bonds were formed with chain A: R287, N344, W343, D316 and chain B: R492 and W519 with Nano-32: D1, N5, S25, L45, S101, and D123. Electrostatic interactions formed between P domain chain A: R287, E236, chain B: D247 and Nano-32: D1 and K120. Hydrophobic interactions involved chain A: P314 and chain B: P518, V248 and Nano-32: V2, L45, Y95, and A119.