Cryo-electron microscopy structures of NLRC4 CARD and ASC CARD filaments, presented by Yang Li of Boston Children's Hospital. The data reveals conserved asymmetric interactions and indicates a unified mechanism for caspase-1 recruitment. The study uses structure modeling to show full-length NLRC4 assembly via separate symmetries.
Use Cases
- Modeling protein filament assembly based on conserved asymmetric interactions described.
- Studying homotypic CARD-CARD interactions in caspase-1 recruitment pathways.
- Comparing assembly patterns between adaptor proteins ASC and NLRC4.
- Validating structure predictions for nucleotide-binding domain (NBD) symmetry.
Strengths
- Structures derived from cryo-electron microscopy, a high-resolution imaging technique.
- Analysis includes three conserved types of asymmetric interactions (types I, II, and III).
- Data connects to a previously defined caspase-1 CARD filament structure for comparison.
Limitations
- Row count and dataset size are 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
- Boston Children's Hospital
- Collection Method
- Cryo-electron microscopy (cryo-EM) imaging and structure modeling.