Summary
In a survey of 95 nanobody-antigen structures, nanobodies bound their antigen in one of three ways, and the majority did not engage with all three CDRs. (1) classified these as: 1) side-on with mostly CDR3 (48%), 2) side-on with both CDRs and framework (34%), and 3) head-on with all three CDRs contributing to binding (18%).
Figures
Ref (1)
See also
- Nanobody CDRH3 loops are longer but more compact
- Nanobody framework residues more likely to be part of paratope than those of antibodies
1.
Ketaren NE, Fridy PC, Malashkevich V, Sanyal T, Brillantes M, Thompson MK, et al. Unique mechanisms to increase structural stability and enhance antigen binding in nanobodies. Structure. 2025;33(4):677-690.e5. Available from: https://doi.org/10.1016/j.str.2025.01.019