| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2025-12-11 |
| タイトル |
|
|
タイトル |
Ligand binding to the membrane-distal domain of Met receptor induces dimerization at the membrane-proximal domain |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 著者 |
Yilmaz Neval
Tanino Hiroki
Flechsig Holger
Sakuraba Shun
Matsumoto Atsushi
Kono Hidetoshi
Puppulin Leonardo
Shibata Mikihiro
Takagi Junichi
Aono Hiroshi
Inoue Tsuyoshi
Matsumoto Kunio
Sakai Katsuya
|
| 抄録 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
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 structural analysis poses two significant challenges: preserving the complex structure during isolation from living cells and achieving high-resolution characterization. In this study, we analyzed the structure of the active complex of the hepatocyte growth factor (HGF)-Met receptor by chemically fixing prior to isolating from living cells and high-speed atomic force microscopy imaging at the single-protein level. We also conducted split-luciferase complementary assay and cryo-electron microscopy experiments for the HGF-Met extracellular domain complex and complemented these results with molecular dynamics simulations. We found that HGF binding to the Sema domain of Met promotes homotypic dimerization at the membrane-proximal region of Met, specifically the IPT4 domain. In summary, our study unveils the structural features of the physiological HGF-Met complex and clarifies the ligand-induced dimerization of the Met receptor. |
| 書誌情報 |
ACS Nano
巻 19,
号 48,
p. 40746-40758,
発行日 2025-11
|
| 出版者 |
|
|
出版者 |
American Chemical Society |
| DOI |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
10.1021/acsnano.4c17358 |
