Cellular Prion Protein Binding Sites for the NMDA Receptor

Experimental data from co-immunoprecipitation, peptide arrays, and protein structure analyses identified two binding sites in the cellular prion protein (PrP^C) for the N-methyl-d-aspartate receptor (NMDA-R). The dataset, 11.1 KB in size, was authored by Joshua E. Mayfield and last updated on March 19, 2026.

Use Cases

• Validate protein-protein interaction models based on the identified N- and C-terminal binding sites.
• Analyze the inhibitory effect of N-linked glycans on binding to the GluN1 subunit.
• Study the interaction mechanisms of membrane-anchored or released PrP^C with NMDA receptors.

Strengths

• Identifies two specific binding sites (N-terminal disordered region and C-terminal α1 helix/β1 strand) within PrP^C.
• Data is derived from targeted experiments including co-immunoprecipitation and peptide arrays.
• File size is 11.1 KB, indicating a focused and likely manageable dataset.

Limitations

• Row count and column-level documentation are unknown, which may limit suitability assessment.
• Data is from a single experimental study using HEK293T cells, which may limit generalizability.

Provenance

Source

figshare

Collection Method

Generated from co-immunoprecipitation, peptide arrays, and protein structure analyses of extracts from transfected HEK293T cells.

Freshness

Last updated 2026-03-19 19:34:11