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- W2044725841 abstract "Gephyrin is a major determinant for the accumulation and anchoring of glycine receptors (GlyRs) and the majority of γ-aminobutyric acid type A receptors (GABAARs) at postsynaptic sites. Here we explored the interaction of gephyrin with a dimeric form of a GlyR β-subunit receptor-derived peptide. A 2 Å crystal structure of the C-terminal domain of gephyrin (GephE) in complex with a 15-residue peptide derived from the GlyR β-subunit defined the core binding site, which we targeted with the dimeric peptide. Biophysical analyses via differential scanning calorimetry (DSC), thermofluor, and isothermal titration calorimetry (ITC) demonstrated that this dimeric ligand is capable of binding simultaneously to two receptor binding sites and that this multivalency results in a 25-fold enhanced affinity. Our study therefore suggests that the oligomeric state of gephyrin and the number of gephyrin-binding subunits in the pentameric GABAARs and GlyRs together control postsynaptic receptor clustering." @default.
- W2044725841 created "2016-06-24" @default.
- W2044725841 creator A5035890430 @default.
- W2044725841 creator A5037176775 @default.
- W2044725841 creator A5082515058 @default.
- W2044725841 date "2014-09-10" @default.
- W2044725841 modified "2023-10-16" @default.
- W2044725841 title "Modulation of Gephyrin-Glycine Receptor Affinity by Multivalency" @default.
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- W2044725841 doi "https://doi.org/10.1021/cb500303a" @default.
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