ABCG2 E211Q Mutant: Cryo-EM Structure with Estrone 3-Sulfate and 5D3-Fab

A cryo-electron microscopy structure of the ABCG2 E211Q mutant protein bound to estrone 3-sulfate and 5D3-Fab, authored by Ioannis Manolaridis of ETH Zurich. The description suggests the data relates to substrate and inhibitor binding, where compound size and affinity are important distinguishing factors. The dataset is available under an Open Access license via the paperswithcode platform.

Use Cases

• Analyzing protein-ligand interactions based on the described binding of estrone 3-sulfate.
• Distinguishing between substrates and inhibitors based on the described importance of compound size and binding affinity.
• Modeling mutant protein structures for the ABCG2 transporter based on the E211Q mutation detail.
• Studying Fab antibody fragment binding to membrane proteins based on the inclusion of 5D3-Fab.

Strengths

• Structure is derived from cryo-electron microscopy, a high-resolution technique.
• Dataset is associated with a specific protein mutant (E211Q) and two bound molecules, providing specificity.
• Data originates from a research institution (ETH Zurich) and is published on an academic platform (paperswithcode).

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

paperswithcode

Collection Method

Cryo-electron microscopy (cryo-EM) structure determination.