BubR1 Kinase Domain Crystal Structure from Drosophila melanogaster

A crystal structure revealing the kinase domain of the Drosophila melanogaster protein BubR1, which was previously thought to be a pseudokinase. The structure was determined by Long Lin and suggests the domain folds into a catalytically active conformation. Computational modeling identified bubristatin as a selective antagonist targeting specific helices of the BubR1 kinase domain.

Use Cases

• Modeling kinase-inhibitor interactions based on the described BubR1 structure and bubristatin binding site.
• Studying the structural basis for the BubR1-mediated phosphorylation switch of CENP-E mentioned in the description.
• Analyzing protein conformation to understand catalytic activity in kinases previously classified as pseudokinases.

Strengths

• Structure reveals a specific catalytically active conformation for the BubR1 kinase domain.
• Description includes a specific computational modeling result identifying the antagonist bubristatin.

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

Long Lin

Collection Method

Crystallography and computational modeling, as described.