DENR-MCT-1 Complex: Crystal Structure of a Human Translation Regulator

A crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR, determined at 2.0-Å resolution. The data elucidates the atomic mechanism of interaction for these proteins, which support noncanonical translation initiation and ribosome recycling. The structure was determined by Ivan B. Lomakin of Yale University.

Use Cases

• Analyzing protein-protein interaction interfaces based on the described heterodimer structure.
• Studying zinc ion-binding sites in proteins based on the conserved cysteine residues (C34, C37, C44, C53) of DENR.
• Modeling the mechanism of translation reinitiation based on the ribosome-binding function of the DENR-MCT-1 complex.

Strengths

• Atomic-resolution structure determined at 2.0-Å resolution.
• Specific identification of four conserved cysteine residues (C34, C37, C44, C53) forming a zinc-binding site essential for dimerization.

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

Ivan B. Lomakin, Yale University

Collection Method

Crystallography