Catching a complex for optimal signaling
Year: 2019
Type: article
Abstract: Agonistic antibodies are powerful tools to dimerize receptors in the absence of ligand binding, but high-fidelity receptor activation requires that these antibodies accurately recapitulate the native dimeric state. Spangler et al. employ a clever approach to select for antibodies that bind a specific IL-4Rα/γ c heterodimeric complex in its native signaling conformation, leading to a monovalent "stapler," a single-chain variable fragment (scFv) that binds at the dimerization interface. This powerful approach can be further exploited for a variety of homo- or heterodimeric receptors to achieve signaling, especially in the absence of endogenous ligand.
Source: Journal of Biological Chemistry
Author: Dirk M. Zajonc
Institution: Pfizer (United States)
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2974698555