ORP1-ORD Crystal Structure with Cholesterol at 2.6 A Resolution

Crystal structure data of the human ORP1-ORD protein domain bound to cholesterol. The data likely contains atomic coordinates and structural parameters from X-ray crystallography experiments. The work by Jiangqing Dong from the Center for Life Sciences unveils a mechanism for PIP-mediated enhancement of cholesterol transport.

Use Cases

• Analyzing protein-ligand interactions based on the cholesterol binding site.
• Studying membrane targeting mechanisms based on the described role in cholesterol extraction.
• Investigating allosteric regulation of lipid transport proteins based on the PIP interaction mechanism.

Strengths

• Atomic resolution of 2.6 Angstroms provides detailed structural information.
• Data is associated with a specific protein-ligand complex (ORP1-ORD with cholesterol).

Limitations

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

Provenance

Source

paperswithcode

Collection Method

X-ray crystallography