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Dimerization effect of sucrose octasulfate on rat FGF1
N Kulahin1, V Kiselyov, A Kochoyan
1Protein Laboratory, Department of Neuroscience and Pharmacology, University of Copenhagen, Copenhagen, Denmark. kulahin@plab.ku.dk
Summary
Sucrose octasulfate (SOS) activates fibroblast growth factor (FGF) signaling. Structural analysis revealed SOS-mediated dimerization of rat FGF1, highlighting key sulfate-binding residues and a unique serine at position 116, potentially influencing dimerization.
Area of Science:
- Biochemistry and Structural Biology
- Molecular Cell Biology
Background:
- Fibroblast growth factors (FGFs) are a family of heparin-binding proteins crucial for regulating cell functions.
- Sucrose octasulfate (SOS), a heparin analogue, is known to activate FGF signaling pathways.
Purpose of the Study:
- To elucidate the structural basis of SOS-mediated activation of FGF signaling.
- To investigate the interaction between rat FGF1 and SOS at the molecular level.
Main Methods:
- X-ray crystallography was employed to determine the structure of rat FGF1 in complex with SOS at 2.2 Å resolution.
- Gel-filtration experiments were conducted to confirm SOS-induced dimerization of FGF1.
Main Results:
- The crystal structure revealed SOS-mediated dimerization of rat FGF1.
- Key residues (Lys113, Lys118, Arg122, Lys128) involved in sulfate binding were identified.
- Rat FGF1 possesses a serine at position 116, unlike the consensus arginine found in other mammalian FGFs, suggesting a role in dimerization.
Conclusions:
- SOS binding induces dimerization of FGF1, a potential mechanism for signal activation.
- Specific amino acid residues and the unique serine at position 116 in rat FGF1 are critical for SOS-mediated dimerization.
