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Single-particle cryo-EM unaligned micrographs of Sevenless extracellular domain (pH 6.6)


ABSTRACT:

SUBMITTER: Cerutti Gabriele 

PROVIDER: EMPIAR-12304 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

Structures and pH-dependent dimerization of the sevenless receptor tyrosine kinase.

Cerutti Gabriele G   Arias Ronald R   Bahna Fabiana F   Mannepalli Seetha S   Katsamba Phinikoula S PS   Ahlsen Goran G   Kloss Brian B   Bruni Renato R   Tomlinson Andrew A   Shapiro Lawrence L  

Molecular cell 20241106 23


Sevenless (Sev) is a Drosophila receptor tyrosine kinase (RTK) required for the specification of the R7 photoreceptor. It is cleaved into α and β 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 activ  ...[more]

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