9bfu
From Proteopedia
Cryo-EM structure of Sevenless extracellular domain (composite map of the dimer, pH 4.6)
Structural highlights
Function7LESS_DROME Receptor for an extracellular signal required to instruct a cell to differentiate into an R7 photoreceptor. The ligand for sev is the boss (bride of sevenless) protein on the surface of the neighboring R8 cell.[1] Publication Abstract from PubMedSevenless (Sev) is a Drosophila receptor tyrosine kinase (RTK) required for the specification of the R7 photoreceptor. It is cleaved into alpha and beta subunits and binds the ectodomain of the G-protein-coupled receptor bride of sevenless (Boss). Previous work showed that the Boss ectodomain could bind but not activate Sev; rather, the whole seven-pass transmembrane Boss was required. Here, we show that Sev does not need to be cleaved to function and that a single-pass transmembrane form of Boss activates Sev. We use cryo-electron microscopy and biophysical methods to determine the structural basis of ligand binding and pH-dependent dimerization of Sev, and we discuss the implications in the process of Sev activation. The Sev human homolog, receptor oncogene from sarcoma 1 (ROS1), is associated with oncogenic transformations, and we discuss their structural similarities. , PMID:39510067[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
