Structural insights into phenylethanolamines high-affinity binding site in NR2B from binding and molecular modeling studies
2008
Understanding How Ifenprodil Binds to NR2B Receptor
publication
Evidence: moderate
Author Information
Author(s): Ng Fui-Mee, Geballe Matthew T, Snyder James P, Traynelis Stephen F, Low Chian-Ming
Primary Institution: National University of Singapore
Hypothesis
The study investigates the structural and functional properties of the ifenprodil binding domain on the NR2B protein.
Conclusion
The study provides evidence that ifenprodil binds to the amino-terminal domain of the NR2B subunit, influencing receptor activity.
Supporting Evidence
- Ifenprodil and its analogues bind to the amino-terminal domain of NR2B.
- Mutations in critical amino acids significantly affect ifenprodil binding affinity.
- The study provides a model for understanding ligand interactions with NMDA receptors.
Takeaway
This study shows how a specific protein part can grab onto a drug, helping us understand how it works in the brain.
Methodology
The study used site-directed mutagenesis, circular dichroism spectroscopy, and molecular modeling to analyze binding interactions.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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