Article
Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.
Open biology - 29 May 2013
Nayeem Naushaba, Mayans Olga, Green Tim
Abstract excerpt
Gating of AMPA- and kainate-selective ionotropic glutamate receptors can be defined in terms of ligand affinity, efficacy and the rate and extent of desensitization. Crucial insights into all three elements have come from structural studies of the ligand-binding domain (LBD). In particular, binding-cleft closure is associated with efficacy, whereas dissociation of the dimer formed by neighbouring LBDs is linked...
Topics
- Animals
- Anions
- Binding Sites
- Chlorides
- Crystallography, X-Ray
- Glutamic Acid
- HEK293 Cells
- Humans
- Kainic Acid
- Ligands
- Mutant Proteins
- Mutation
- Phenotype
- Protein Binding
- Protein Multimerization
- Protein Structure, Tertiary
- Rats
- Receptors, Kainic Acid