Cellular Prion Protein Binding Sites for the NMDA Receptor

Joshua E. Mayfield's research data from 2026 identifies two specific binding sites in the cellular prion protein (PrP^C) for the NMDA receptor. The dataset, 30.3 KB in size, is derived from co-immunoprecipitation experiments, peptide arrays, and protein structure analyses using HEK293T cells. It is shared under a CC-BY-NC-4.0 license on figshare.

Use Cases

• Validate protein-protein interaction models based on identified N- and C-terminal binding sites.
• Analyze the inhibitory effect of N-linked glycans on GluN1 binding based on glycosylation site data.
• Study the role of the PrP^C P3 peptide sequence in NMDA receptor interaction.
• Investigate the structural basis of PrP^C binding to GluN1–GluN2B complexes versus isolated GluN1.

Strengths

• Data is derived from a targeted series of experimental methods including co-immunoprecipitation and peptide arrays.
• Identifies two specific binding sites (N-terminal disordered region and C-terminal α1 helix/β1 strand) with functional implications.
• File format is XLSX, which is widely accessible for analysis.

Limitations

• Dataset is very small at 30.3 KB, indicating limited scope.
• Row count and column-level documentation are unknown, requiring manual inspection after download.
• Description metadata is limited; actual data quality requires manual inspection after download.

Provenance

Source

figshare

Collection Method

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

Freshness

Last updated 2026-03-19 19:34:09; freshness should be verified.