Amino Terminal Domains of the NMDA Receptor Are Organized as Local Heterodimers
2011
NMDA Receptor ATDs Are Local Heterodimers
publication
Evidence: moderate
Author Information
Author(s): Lee Chia-Hsueh, Gouaux Eric
Primary Institution: Oregon Health and Science University
Hypothesis
Do NMDA receptor ATDs form architecturally similar local dimers?
Conclusion
The study demonstrates that GluN1 and GluN2 ATDs form local heterodimers through interactions in the L1-L1 interface.
Supporting Evidence
- GluN1 and GluN2 ATDs spontaneously formed disulfide bond-mediated dimers.
- The formation of dimer could be prevented by knocking out endogenous cysteines.
- Cross-linking experiments confirmed the heterodimer formation between GluN1 and GluN2 ATDs.
Takeaway
The parts of the NMDA receptor that help it work together can stick to each other in a special way, like puzzle pieces fitting together.
Methodology
The organization of the amino terminal domain of NMDA receptors was studied using cysteine-directed, disulfide bond-mediated cross-linking.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website