NMR Structure of the Calcium-Bound EGF-Like Domain in Coagulation Factor X

A three-dimensional structure determined by two-dimensional NMR and simulated folding for the calcium-bound form of the NH2-terminal epidermal growth factor (EGF)-like domain in coagulation factor X. The research was conducted by M Selander-Sunnerhagen of Lund University. The dataset likely contains structural coordinates and ligand information for the calcium ion binding site.

Use Cases

• Modeling calcium binding sites in EGF-like domains based on identified ligand residues.
• Comparing protein structures between calcium-bound and calcium-free forms based on described local structural changes.
• Studying conserved residues for calcium binding in proteins like Notch and TAN-1 based on mentioned sequence conservation.

Strengths

• Structure determined by two-dimensional NMR, providing high-resolution atomic-level detail.
• Specific calcium ion ligands are identified, including Gly-47, Gly-64, Gln-49, and erythro-beta-hydroxyaspartic acid 63.
• Includes a comparison with the calcium-free form, highlighting induced structural changes.

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

paperswithcode, authored by M Selander-Sunnerhagen of Lund University.

Collection Method

Two-dimensional NMR spectroscopy and simulated folding.