A comprehensive analysis of novel disulfide bond introduction site into the constant domain of human Fab
Abstract Generally, intermolecular disulfide bond contribute to the conformational protein stability. To identify sites where intermolecular disulfide bond can be introduced into the Fab’s constant domain of the therapeutic IgG, Fab mutants were predicted using the MOE software, a molecular simulato...
Guardado en:
Autores principales: | Hitomi Nakamura, Moeka Yoshikawa, Naoko Oda-Ueda, Tadashi Ueda, Takatoshi Ohkuri |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/bd98ac20ab994f19be7387966c045670 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The structure-function relationship of disulfide bonds in etanercept
por: William C. Lamanna, et al.
Publicado: (2017) -
The disulfide bond Cys2724-Cys2774 in the C-terminal cystine knot domain of von Willebrand factor is critical for its dimerization and secretion
por: Yuxin Zhang, et al.
Publicado: (2021) -
A single disulfide bond disruption in the β3 integrin subunit promotes thiol/disulfide exchange, a molecular dynamics study.
por: Lihie Levin, et al.
Publicado: (2013) -
General synthetic strategy for regioselective ultrafast formation of disulfide bonds in peptides and proteins
por: Shay Laps, et al.
Publicado: (2021) -
DutaFabs are engineered therapeutic Fab fragments that can bind two targets simultaneously
por: Roland Beckmann, et al.
Publicado: (2021)