Fig. 5: Submolecular probing of the kinetic and thermodynamic parameters underlying C5a ligand binding to C5aR. | Communications Biology

Fig. 5: Submolecular probing of the kinetic and thermodynamic parameters underlying C5a ligand binding to C5aR.

From: Submolecular probing of the complement C5a receptor–ligand binding reveals a cooperative two-site binding mechanism

Fig. 5

DFS plots showing the loading rate-dependent interaction forces of the C5a ligand probed against wild-type C5aR (a) and C5aRD282A (b). c, d Probing the kinetic and thermodynamic parameters underlying C5a ligand binding to the orthosteric binding sites. The binding site (c) was probed using C5aR complexed in presence of the PMX53 antagonist. To access the effector site (d), C5a was probed with C5aR missing a Tyr residue at the N-terminal end. Fitting the data using the Friddle–Noy–de Yoreo model (thin lines) provides Feq, ΔGbu, and residence time (τ0.5) values with errors representing the s.e.m. Each circle represents one measurement. Darker shaded areas represent 99% confidence intervals, and lighter shaded areas represent 99% of prediction intervals. For each condition, data are representative of at least three independent experiments.

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