The A391E mutation enhances FGFR3 activation in the absence of ligand.

doi:10.1016/j.bbamem.2011.04.007

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Article

The A391E mutation enhances FGFR3 activation in the absence of ligand.

Biochimica et biophysica acta - 1 Aug 2011

Chen Fenghao, Degnin Catherine, Laederich Melanie, Horton William A, Hristova Kalina

Abstract excerpt

The A391E mutation in the transmembrane domain of fibroblast growth factor receptor 3 leads to aberrant development of the cranium. It has been hypothesized that the mutant glutamic acid stabilizes the dimeric receptor due to hydrogen bonding and enhances its ligand-independent activation. We previously tested this hypothesis in lipid bilayers and showed that the mutation stabilizes the isolated transmembrane...

Topics

Cell Membrane
Fibroblast Growth Factor 1
HEK293 Cells
Humans
Hydrogen Bonding
Ligands
Models, Biological
Models, Chemical
Mutation
Phosphorylation
Protein Multimerization
Protein Stability
Receptor, Fibroblast Growth Factor, Type 3
Structure-Activity Relationship

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Identifiers

PMID: 21536014
DOI: 10.1016/j.bbamem.2011.04.007
PMCID: PMC3110564

Genes

FGFR3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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