Ligand Binding to the Membrane-Distal Domain of the Met Receptor Induces Dimerization at the Membrane-Proximal Domain

Activation of cytokine and growth factor receptors by ligands triggers crucial cellular responses in various physiological processes. However, our understanding of their structural basis remains incomplete due to the limited information on the active ligand–receptor complex structure. Their structur...

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Detalles Bibliográficos
Autor principal:	Neval Yilmaz (1544557) (author)
Otros Autores:	Hiroki Tanino (22686882) (author), Shun Sakuraba (1368381) (author), Romain Amyot (9657017) (author), Holger Flechsig (213426) (author), Atsushi Matsumoto (593817) (author), Hidetoshi Kono (19475) (author), Leonardo Puppulin (11688279) (author), Mikihiro Shibata (2075461) (author), Hiroshi Aoyama (832169) (author), Tsuyoshi Inoue (559318) (author), Kunio Matsumoto (412408) (author), Katsuya Sakai (11688282) (author)
Publicado:	2025
Materias:	Biophysics Biochemistry Cell Biology Molecular Biology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified molecular dynamics simulations luciferase complementary assay hepatocyte growth factor growth factor receptors electron microscopy experiments chemically fixing prior also conducted split various physiological processes proximal domain activation proximal region sema domain ipt4 domain distal domain physiological hgf structural features resolution characterization protein level living cells limited information induced dimerization active complex
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Ligand Binding to the Membrane-Distal Domain of the Met Receptor Induces Dimerization at the Membrane-Proximal Domain

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