The extracellular domains of ErbB3 retain high ligand binding affinity at endosome pH and in the locked conformation.

Abstract excerpt

The extracellular, ligand binding regions of ErbB receptors consist of four domains that can assume at least two alternative conformations, extended and locked. The locked conformation, observed in several crystal structures, is held together by a noncovalent intramolecular tether and is incompatible with current models for receptor dimerization and ligand activation. Based on structures of ligand-receptor...

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