Regulation of Receptor Binding Specificity of FGF9 by an Autoinhibitory Homodimerization
July 2017
in “
Structure
”
Fibroblast Growth Factor 9 FGF9 receptor binding specificity autoinhibitory homodimerization FGFR1c FGFR2c FGFR3c D195A substitution hydrophobic interactions water-mediated hydrogen bonds Pfeiffer craniosynostosis syndrome multiple synostosis syndrome receptor binding homodimerization D195A mutation hydrogen bonds Pfeiffer syndrome synostosis syndrome
Studysummary In this study, researchers found that ligand homodimerization controls the receptor binding specificity of the FGF9 subfamily, preventing off-target activation of FGFR "b" isoforms.
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