6P79

Engineered single chain antibody C9+C14 ScFv

6P79 の概要

• エントリーDOI: 10.2210/pdb6p79/pdb
• 分子名称: Engineered antibody heavy chain, Engineered antibody light chain (3 entities in total)
• 機能のキーワード: antibody engineering, immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26798.67

構造登録者

Zhang, Y.,Li, W.,Marshall, N. (登録日: 2019-06-05, 公開日: 2020-04-15, 最終更新日: 2024-10-30)

主引用文献

Lee, J.,Der, B.S.,Karamitros, C.S.,Li, W.,Marshall, N.M.,Lungu, O.I.,Miklos, A.E.,Xu, J.,Kang, T.H.,Lee, C.H.,Tan, B.,Hughes, R.A.,Jung, S.T.,Ippolito, G.C.,Gray, J.J.,Zhang, Y.,Kuhlman, B.,Georgiou, G.,Ellington, A.D.
Computer-based Engineering of Thermostabilized Antibody Fragments.
Aiche J, 66:-, 2020

PubMed Abstract: We used the molecular modeling program Rosetta to identify clusters of amino acid substitutions in antibody fragments (scFvs and scAbs) that improve global protein stability and resistance to thermal deactivation. Using this methodology, we increased the melting temperature (T) and resistance to heat treatment of an antibody fragment that binds to the hemagglutinin protein (anti-HA33). Two designed antibody fragment variants with two amino acid replacement clusters, designed to stabilize local regions, were shown to have both higher T compared to the parental scFv and importantly, to retain full antigen binding activity after 2 hours of incubation at 70 °C. The crystal structure of one thermostabilized scFv variants was solved at 1.6 Å and shown to be in close agreement with the RosettaAntibody model prediction.

PubMed: 32336757
DOI: 10.1002/aic.16864

実験手法

X-RAY DIFFRACTION (1.583 Å)