DNMT1 RFTS Domain Complex with Ubiquitin: Crystal Structure Data

Crystal structure data of the DNMT1 RFTS domain in complex with ubiquitin, highlighting a unique ubiquitin binding mode. The dataset, from an open-access paper by C. Qian of the University of Hong Kong, provides evidence for distinct binding interactions between DNMT1 and domains of UHRF1. It supports the study of regulatory mechanisms for DNMT1 activation and DNA methylation maintenance.

Use Cases

• Analyzing ubiquitin binding modes based on the presented crystal structure.
• Studying protein-protein interactions between DNMT1 and UHRF1 domains.
• Modeling the impact of specific domain interactions on DNMT1 enzymatic activity.
• Investigating the structural basis for DNMT1 localization to replication foci.

Strengths

• Data originates from a crystal structure study, providing atomic-level detail.
• The description details specific molecular interactions, such as between the RFTS domain and ubiquitin.

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

University of Hong Kong

Collection Method

Crystallography