Mouse Cryptochrome 1 Crystal Structure with TH301 Compound

Crystal structure data from Nagoya University research on mouse Cryptochrome 1 (CRY1) in complex with the selective stabilizer compound TH301. The dataset likely contains atomic coordinates and structural information derived from X-ray crystallography experiments. The research aimed to understand isoform-specific functions of circadian clock proteins.

Use Cases

• Analyzing protein-compound binding interactions based on the described crystal structure.
• Studying isoform selectivity mechanisms in cryptochrome proteins based on the described C-terminal region involvement.
• Investigating the structural basis for circadian clock modulation based on the described compound-binding sites.

Strengths

• Data originates from a specific research institution (Nagoya University).
• Focuses on a defined protein-compound complex (CRY1-TH301) with a described biological context.

Limitations

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

Provenance

Source

Nagoya University

Collection Method

X-ray crystallography from phenotypic screening research.