Structure of the Tandem Fibronectin Type 3 Domains of Neural Cell Adhesion Molecule
2008
Structure of the NCAM Fibronectin Type 3 Domains
publication
Evidence: moderate
Author Information
Author(s): Federico Carafoli, Jane L. Saffell, Erhard Hohenester
Primary Institution: Imperial College London
Hypothesis
How do the fibronectin type 3 domains of NCAM interact with FGFR1?
Conclusion
The NCAM–FGFR1 interaction at the cell surface may be transient or stabilized by receptor clustering.
Supporting Evidence
- The crystal structure revealed an acutely bent domain arrangement.
- Mutations in NCAM affected its conformation and potential binding to FGFR1.
- Surface plasmon resonance experiments showed a very weak interaction between NCAM and FGFR1.
Takeaway
This study looks at how a protein called NCAM bends and interacts with another protein, FGFR1, which is important for nerve growth.
Methodology
The crystal structure of the NCAM FN3 tandem was determined using X-ray crystallography.
Limitations
The weak interaction observed may not reflect the physiological conditions due to differences in glycosylation of proteins used.
Statistical Information
P-Value
> 100 μM
Digital Object Identifier (DOI)
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