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Article

Dimer Interface in Natural Variant NK1 Is Dispensable for HGF-Dependent Met Receptor Activation.

International journal of molecular sciences - 26 Aug 2021

Tahira Yumiko, Sakai Katsuya, Sato Hiroki, Imamura Ryu, Matsumoto Kunio

Abstract excerpt

NK1, a splicing variant of hepatocyte growth factor (HGF), binds to and activates Met receptor by forming an NK1 dimer and 2:2 complex with Met. Although the structural mechanism underlying Met activation by HGF remains incompletely resolved, it has been proposed that the NK1 dimer structure participates in this activation. We investigated the NK1 dimer interface's role in Met activation by HGF. Because N127,...

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Identifiers

PMID: 34502141
DOI: 10.3390/ijms22179240
PMCID: PMC8431453

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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