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

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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Dettagli Bibliografici
Autore principale: Neval Yilmaz (1544557) (author)
Altri autori: 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)
Pubblicazione: 2025
Soggetti:
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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