6IH9
Adeno-Associated Virus 2 at 2.8 ang
Summary for 6IH9
| Entry DOI | 10.2210/pdb6ih9/pdb |
| EMDB information | 9671 |
| Descriptor | Capsid protein VP1 (1 entity in total) |
| Functional Keywords | aav2, virus |
| Biological source | Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2) |
| Total number of polymer chains | 1 |
| Total formula weight | 58644.49 |
| Authors | |
| Primary citation | Zhang, R.,Cao, L.,Cui, M.,Sun, Z.,Hu, M.,Zhang, R.,Stuart, W.,Zhao, X.,Yang, Z.,Li, X.,Sun, Y.,Li, S.,Ding, W.,Lou, Z.,Rao, Z. Adeno-associated virus 2 bound to its cellular receptor AAVR. Nat Microbiol, 4:675-682, 2019 Cited by PubMed Abstract: Adeno-associated virus (AAV) is a leading vector for virus-based gene therapy. The receptor for AAV (AAVR; also named KIAA0319L) was recently identified, and the precise characterization of AAV-AAVR recognition is in immediate demand. Taking advantage of a particle-filtering algorithm, we report here the cryo-electron microscopy structure of the AAV2-AAVR complex at 2.8 Å resolution. This structure reveals that of the five Ig-like polycystic kidney disease (PKD) domains in AAVR, PKD2 binds directly to the spike region of the AAV2 capsid adjacent to the icosahedral three-fold axis. Residues in strands B and E, and the BC loop of AAVR PKD2 interact directly with the AAV2 capsid. The interacting residues in the AAV2 capsid are mainly in AAV-featured variable regions. Mutagenesis of the amino acids at the AAV2-AAVR interface reduces binding activity and viral infectivity. Our findings provide insights into the biology of AAV entry with high-resolution details, providing opportunities for the development of new AAV vectors for gene therapy. PubMed: 30742069DOI: 10.1038/s41564-018-0356-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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