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A two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing

Sarah E. Adams, Andrew G. Purkiss, Phillip P. Knowles, Andrea Nans, David C. Briggs, Annabel Borg, Christopher Earl, K.M. Goodman, Agata Nawrotek, Aaron J. Borg, Pauline B. McIntosh, Francesca Houghton, Svend Kjær, Neil Q. McDonald

2021Structure14 citationsDOIOpen Access PDF

Abstract

-GDNF-GFRα1a suggesting that a conserved contact stabilizes higher-order species. Our study reveals that ligand-co-receptor recognition by RET involves both receptor plasticity and strict spacing of receptor dimers by GFL ligands.

Topics & Concepts

Glial cell line-derived neurotrophic factorReceptorReceptor tyrosine kinaseBiophysicsLigand (biochemistry)BiologyCell biologyChemistryBiochemistryNeurotrophic factorsProtein Structure and DynamicsSignaling Pathways in DiseaseReceptor Mechanisms and Signaling
A two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing | Litcius