A cryo-electron microscopy structure of the Adeno-associated virus 2 (AAV2) complexed with its receptor (AAVR) at 2.8 Å resolution. The data was produced by researchers from Tsinghua University to characterize the precise recognition interface between the viral capsid and the receptor's PKD2 domain. The structure reveals interacting residues, and mutagenesis studies confirm their role in binding and viral infectivity.
Use Cases
- Modeling protein-protein interactions based on the high-resolution AAV2-AAVR interface.
- Informing the design of engineered AAV vectors based on capsid residues in variable regions.
- Studying viral entry biology using the detailed structural insights into the spike region binding site.
Strengths
- High-resolution structural data at 2.8 Å.
- Includes mutagenesis validation of the identified binding interface.
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
- Z.Y. Lou, Tsinghua University
- Collection Method
- Cryo-electron microscopy with particle-filtering algorithms.