Fig. 5 | Nature Communications

Fig. 5

From: Selection of immunoglobulin elbow region mutations impacts interdomain conformational flexibility in HIV-1 broadly neutralizing antibodies

Fig. 5

Antibody structure and CH103 Fab elbow flexibility. a Surface representation of an IgG antibody. The heavy chain (blue) and light chain (green) pair in the Fab region made up of the antigen binding Fv region and the CH1/CL region leading to the heavy chain pairing Fc region. b Cartoon representation of an IgG antibody. The portion of the structure connecting the CH1/CL region to the Fc region is a site of flexibility termed the antibody hinge. c Top: Additional antibody hinge point between the Fab Fv and CH1/CL region termed the Fab elbow. Bottom: Fab Fv VH and VL orientation flexibility about two planes. d Structural alignment of the CH103 and CH103 UCA crystal structures’ (PDB ID 4JAM chains H and L and 4QHK chains O and P, respectively) CH1/CL region depicting the elbow angle differences. e Elbow angle distribution for the five 1 μs simulations of the CH103 UCA (solid) and the CH103 UCA-P14S/S30G mutant (dashed). f RMSD to the CH103 bnAb (PDB ID 4JAM) distribution for the five 1 μs simulations of the CH103 UCA (solid) and the CH103 UCA-P14S/S30G mutant (dashed). g Structural superposition of the CH103 UCA and CH103 UCA-P14S/S30G onto a CH505TF SOSIP timer homology model based upon the CH103 bound gp120 configuration. h Aggregate simulation VH RMSF difference between the CH103 UCA-P14S/S30G mutant and the CH103 UCA. Dotted lines indicate one standard deviation from the mean. Red brackets indicate HCDR positions. (i) Aggregate simulation VL RMSF difference between the CH103 UCA-P14S/S30G mutant and the CH103 UCA. Dotted lines indicate one standard deviation from the mean. Blue brackets indicate LCDR positions

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