Ontology highlight
ABSTRACT:
SUBMITTER: Opatowsky Y
PROVIDER: S-EPMC3918759 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Opatowsky Yarden Y Lax Irit I Tomé Francisco F Bleichert Franziska F Unger Vinzenz M VM Schlessinger Joseph J
Proceedings of the National Academy of Sciences of the United States of America 20140121 5
Using electron microscopy and fitting of crystal structures, we present the 3D reconstruction of ligand-induced dimers of intact receptor tyrosine kinase, KIT. We observe that KIT protomers form close contacts throughout the entire structure of ligand-bound receptor dimers, and that the dimeric receptors adopt multiple, defined conformational states. Interestingly, the homotypic interactions in the membrane proximal Ig-like domain of the extracellular region differ from those observed in the cry ...[more]