Article
The micromolar zinc-binding domain on the NMDA receptor subunit NR2B.
The Journal of neuroscience : the official journal of the Society for Neuroscience - 12 Jan 2005
Rachline Julie, Perin-Dureau Florent, Le Goff Anne, Neyton Jacques, Paoletti Pierre
Abstract excerpt
Eukaryotic ionotropic glutamate receptor subunits possess a large N-terminal domain (NTD) distinct from the neighboring agonist-binding domain. In NMDA receptors, the NTDs of NR2A and NR2B form modulatory domains binding allosteric inhibitors. Despite a high sequence homology, these two domains have been shown to bind two ligands of strikingly different chemical nature. Whereas the NTD of NR2A binds zinc with...
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Binding Sites
- Binding, Competitive
- Ligands
- Molecular Sequence Data
- Mutation
- Piperidines
- Protein Structure, Tertiary
- Receptors, N-Methyl-D-Aspartate
