Fyn SH3 Domain Crystal Structure at 1.9 Å Resolution

1.9 Å resolution crystal structure of the SH3 domain from the human Fyn tyrosine kinase, reported by M.E.M. Noble of the European Molecular Biology Organization. The dataset compares the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin, identifying a conserved surface patch flanked by variable loops. The crystals contain two SH3 molecules per asymmetric unit.

Use Cases

• Predicting protein-protein interaction interfaces based on the conserved aromatic surface patch.
• Comparative structural analysis of SH3 domain evolution between tyrosine kinases and spectrin.
• Modeling loop region flexibility and its role in modulating binding specificity.

Strengths

• High-resolution structural data at 1.9 Å.
• Direct comparison of SH3 domain structures from two protein families (tyrosine kinases and spectrin).
• Crystal structure includes two molecules per asymmetric unit, providing potential insights into packing interactions.

Limitations

• Row count and specific column-level data are unknown, limiting suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

European Molecular Biology Organization

Collection Method

X-ray crystallography