Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge

β-tryptases are responsible for most of the proteolytic activity during mast cell activation. Here, the authors develop β-tryptase-inhibiting antibodies and provide structural and biochemical evidence that the bivalency of the antibodies is a prerequisite for their inhibitory activity.

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Detalles Bibliográficos
Autores principales: Henry R. Maun, Rajesh Vij, Benjamin T. Walters, Ashley Morando, Janet K. Jackman, Ping Wu, Alberto Estevez, Xiaocheng Chen, Yvonne Franke, Michael T. Lipari, Mark S. Dennis, Daniel Kirchhofer, Claudio Ciferri, Kelly M. Loyet, Tangsheng Yi, Charles Eigenbrot, Robert A. Lazarus, James T. Koerber
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/731be2a1b0e94f0d9e6e6bb1c65b39da
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Descripción
Sumario:β-tryptases are responsible for most of the proteolytic activity during mast cell activation. Here, the authors develop β-tryptase-inhibiting antibodies and provide structural and biochemical evidence that the bivalency of the antibodies is a prerequisite for their inhibitory activity.