Fig. 5: Principles learned from bovine antibodies with ultra-long CDRs. | Nature Communications

Fig. 5: Principles learned from bovine antibodies with ultra-long CDRs.

From: Mechanistic principles of an ultra-long bovine CDR reveal strategies for antibody design

Fig. 5: Principles learned from bovine antibodies with ultra-long CDRs.The alternative text for this image may have been generated using AI.

a. An optimal stalk length in the ultra-long CDR-H3 ensures proper folding without steric clashes between the knob and residues in the variable domains. b There is a consensus between the stalk of CDR-H3 with some of the other CDRs. Depicted are part of the variable domains of NC-Cow1 (PDB:6OO0). The bovine stalk in CDR-H3 is in red, the remaining of the VH domain is in green, the VL domain is in gray. The black lines illustrate a network of potential contacts between the residues in the stalk and some of the other CDRs. c The disulfide bonds (yellow lines) in the ultra-long CDR-H3 (blue) provide conformational restraints crucial for binding to the antigen (magenta).

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