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TitleStructural basis of the activation of c-MET receptor.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4074, Year 2021
Publish dateJul 1, 2021
AuthorsEmiko Uchikawa / Zhiming Chen / Guan-Yu Xiao / Xuewu Zhang / Xiao-Chen Bai /
PubMed AbstractThe c-MET receptor is a receptor tyrosine kinase (RTK) that plays essential roles in normal cell development and motility. Aberrant activation of c-MET can lead to both tumors growth and metastatic ...The c-MET receptor is a receptor tyrosine kinase (RTK) that plays essential roles in normal cell development and motility. Aberrant activation of c-MET can lead to both tumors growth and metastatic progression of cancer cells. C-MET can be activated by either hepatocyte growth factor (HGF), or its natural isoform NK1. Here, we report the cryo-EM structures of c-MET/HGF and c-MET/NK1 complexes in the active state. The c-MET/HGF complex structure reveals that, by utilizing two distinct interfaces, one HGF molecule is sufficient to induce a specific dimerization mode of c-MET for receptor activation. The binding of heparin as well as a second HGF to the 2:1 c-MET:HGF complex further stabilize this active conformation. Distinct to HGF, NK1 forms a stable dimer, and bridges two c-METs in a symmetrical manner for activation. Collectively, our studies provide structural insights into the activation mechanisms of c-MET, and reveal how two isoforms of the same ligand use dramatically different mechanisms to activate the receptor.
External linksNat Commun / PubMed:34210960 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 5.0 Å
Structure data

23919

7mo7

EMDB-23919, PDB-7mo7:
Cryo-EM structure of 2:2 c-MET/HGF holo-complex
Method: EM (single particle) / Resolution: 4.8 Å

23920

7mo8

EMDB-23920, PDB-7mo8:
Cryo-EM structure of 1:1 c-MET I/HGF I complex after focused 3D refinement of holo-complex
Method: EM (single particle) / Resolution: 4.5 Å

23921

7mo9

EMDB-23921, PDB-7mo9:
Cryo-EM map of the c-MET II/HGF I/HGF II (K4 and SPH) sub-complex
Method: EM (single particle) / Resolution: 4.0 Å

23922

7moa

EMDB-23922, PDB-7moa:
Cryo-EM structure of the c-MET II/HGF I complex bound with HGF II in a rigid conformation
Method: EM (single particle) / Resolution: 4.9 Å

23923

7mob

EMDB-23923, PDB-7mob:
Cryo-EM structure of 2:2 c-MET/NK1 complex
Method: EM (single particle) / Resolution: 5.0 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / c-MET / HGF / receptor tyrosine kinase

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