Pub. Date : 1993 Dec 13
PMID : 7903251
3 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | To elucidate the role of disulfide bridges for the allosteric interaction of these agonists we mutated the cysteine residues in the ligand-binding NMDAR1 (NR1 or zeta) subunit of the rodent NMDA receptor and co-expressed the resulting mutants with the NR2B (epsilon 2) subunit in Xenopus oocytes. | Cysteine | glutamate ionotropic receptor NMDA type subunit 1 L homeolog | Xenopus laevis |
| 2 | To elucidate the role of disulfide bridges for the allosteric interaction of these agonists we mutated the cysteine residues in the ligand-binding NMDAR1 (NR1 or zeta) subunit of the rodent NMDA receptor and co-expressed the resulting mutants with the NR2B (epsilon 2) subunit in Xenopus oocytes. | Cysteine | glutamate ionotropic receptor NMDA type subunit 1 L homeolog | Xenopus laevis |
| 3 | These cysteine residues in the putative extracellular domain of the NR1 subunit may form a disulfide bridge important for agonist interaction. | Cysteine | glutamate ionotropic receptor NMDA type subunit 1 L homeolog | Xenopus laevis |