抗体
亲缘关系
化学
结合亲和力
单域抗体
动力学
残留物(化学)
立体化学
计算生物学
生物化学
生物
受体
遗传学
物理
量子力学
作者
Koichi Yamamoto,Satoru Nagatoishi,Makoto Nakakido,Daisuke Kuroda,Kouhei Tsumoto
标识
DOI:10.1016/j.bbrc.2024.149839
摘要
Single-domain VHH antibody is regarded as one of the promising antibody classes for therapeutic and diagnostic applications. VHH antibodies have amino acids in framework region 2 that are distinct from those in conventional antibodies, such as the Val37Phe/Tyr (V37F/Y) substitution. Correlations between the residue type at position 37 and the conformation of the CDR3 in VHH antigen recognition have been previously reported. However, few studies focused on the meaning of harboring two residue types in position 37 of VHH antibodies, and the concrete roles of Y37 have been little to be elucidated. Here, we investigated the functional states of position 37 in co-crystal structures and performed analyses of three model antibodies with either F or Y at position 37. Our analysis indicates that Y at position 37 enhances the dissociation rate, which is highly correlated with drug efficacy. Our findings help to explain the molecular mechanisms that distinguish VHH antibodies from conventional antibodies.
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