Do antibody CDR loops change conformation upon binding?
ABSTRACTAntibodies have increasingly been developed as drugs with over 100 now licensed in the US or EU. During development, it is often necessary to increase or reduce the affinity of an antibody and rational attempts to do so rely on having a structure of the antibody-antigen complex often obtaine...
Main Authors: | Chu’nan Liu, Lilian M. Denzler, Oliver E.C. Hood, Andrew C.R. Martin |
---|---|
Format: | Article |
Language: | English |
Published: |
Taylor & Francis Group
2024-12-01
|
Series: | mAbs |
Subjects: | |
Online Access: | https://www.tandfonline.com/doi/10.1080/19420862.2024.2322533 |
Similar Items
-
Corrigendum: Higher Affinity Antibodies Bind With Lower Hydration and Flexibility in Large Scale Simulations
by: Mabel T. Y. Wong, et al.
Published: (2022-07-01) -
Higher Affinity Antibodies Bind With Lower Hydration and Flexibility in Large Scale Simulations
by: Mabel T. Y. Wong, et al.
Published: (2022-05-01) -
The Structural Basis of Antibody-Antigen Recognition
by: Inbal eSela-Culang, et al.
Published: (2013-10-01) -
A window into the human immune system: comprehensive characterization of the complexity of antibody complementary-determining regions in functional antibodies
by: Oscar Mejias-Gomez, et al.
Published: (2023-12-01) -
Hiding in plain sight: structure and sequence analysis reveals the importance of the antibody DE loop for antibody-antigen binding
by: Simon P. Kelow, et al.
Published: (2020-01-01)