Human GluN1/GluN2A NMDA Receptor Cryo-EM Structures at pH 7.8 and 6.3

Cryo-electron microscopy structures of the human GluN1-GluN2A NMDA receptor solved at pH 7.8 and pH 6.3 by Jinbao Zhang of the Chinese Academy of Sciences. The data reveals the structural basis for proton modulation of receptor activity, showing conformational changes in the N-terminal domain. The findings are supported by molecular dynamics simulations.

Use Cases

• Modeling proton sensor mechanisms based on the described N-terminal domain conformational changes.
• Simulating allosteric coupling between sensor and channel gate using the provided structural coordinates.
• Comparing receptor conformations under different pH conditions as described in the study.

Strengths

• Structures solved at two distinct pH conditions (7.8 and 6.3) enabling comparative analysis.
• Conformational mobility is supported by molecular dynamics simulation as mentioned in the description.
• Data originates from a peer-reviewed scientific study published on an open-access platform.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Jinbao Zhang, Chinese Academy of Sciences

Collection Method

Cryo-electron microscopy and molecular dynamics simulation