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Article

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.

Molecular cell - 7 Sept 2007

Chen Huaibin, Ma Jinghong, Li Wanqing, Eliseenkova Anna V, Xu Chongfeng, Neubert Thomas A, Miller W Todd, Mohammadi Moosa

Abstract excerpt

Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory "molecular brake" mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural...

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Topics

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Share to Phosphorylation
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Hydrogen Bonding

Share to Models, Molecular

Share to Protein Structure, Tertiary

Share to Receptor, Fibroblast Growth Factor, Type 2

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 17803937
DOI: 10.1016/j.molcel.2007.06.028
PMCID: PMC2094128

Genes

FGFR2
FLT3
KIT
TEK

Provenance

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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