Cryo-EM structures of inhibitory antibodies complexed with arginase 1 provide insight into mechanism of action

Cryo-EM structures of inhibitory antibodies complexed with arginase 1 provide insight into mechanism of action

Palte et al provide cryo-EM structures of five potent and inhibitory monoclonal antibodies bound to human Arginase 1, a T-cell modulating metalloenzyme and a cancer drug target. They provide structural insights that will aid in the evaluation of these antibodies as therapeutic inhibitors of arginase...

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Autores principales: Rachel L. Palte, Veronica Juan, Yacob Gomez-Llorente, Marc Andre Bailly, Kalyan Chakravarthy, Xun Chen, Daniel Cipriano, Laurence Fayadat-Dilman, Symon Gathiaka, Heiko Greb, Brian Hall, Mas Handa, Mark Hsieh, Esther Kofman, Heping Lin, J. Richard Miller, Nhung Nguyen, Jennifer O’Neil, Hussam Shaheen, Eric Sterner, Corey Strickland, Angie Sun, Shane Taremi, Giovanna Scapin
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Biology (General)
QH301-705.5
Acceso en línea:https://doaj.org/article/fbf41ee3e220482a9ea5fcab675f2be6
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Sumario:Palte et al provide cryo-EM structures of five potent and inhibitory monoclonal antibodies bound to human Arginase 1, a T-cell modulating metalloenzyme and a cancer drug target. They provide structural insights that will aid in the evaluation of these antibodies as therapeutic inhibitors of arginasemediated T-cell suppression.

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