EMD-9795

Single-particle
3.07 Å
EMD-9795 Deposition: 30/01/2019
Map released: 23/10/2019
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-9795

AAV1 in neutral condition at 3.07 Ang

EMD-9795

Single-particle
3.07 Å
EMD-9795 Deposition: 30/01/2019
Map released: 23/10/2019
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Adeno-associated virus - 1
Sample: Adeno-associated virus - 1
Fitted models: 6jcr (Avg. Q-score: 0.452)

Deposition Authors: Lou Z , Zhang R
Divergent engagements between adeno-associated viruses with their cellular receptor AAVR.
Zhang R, Xu G, Cao L, Sun Z, He Y, Cui M , Sun Y, Li S, Li H, Qin L, Hu M, Yuan Z, Rao Z, Ding W, Rao Z, Lou Z
(2019) Nat Commun , 10 , 3760 - 3760
PUBMED: 31434885
DOI: doi:10.1038/s41467-019-11668-x
ISSN: 2041-1723
Abstract:
Adeno-associated virus (AAV) receptor (AAVR) is an essential receptor for the entry of multiple AAV serotypes with divergent rules; however, the mechanism remains unclear. Here, we determine the structures of the AAV1-AAVR and AAV5-AAVR complexes, revealing the molecular details by which PKD1 recognizes AAV5 and PKD2 is solely engaged with AAV1. PKD2 lies on the plateau region of the AAV1 capsid. However, the AAV5-AAVR interface is strikingly different, in which PKD1 is bound at the opposite side of the spike of the AAV5 capsid than the PKD2-interacting region of AAV1. Residues in strands F/G and the CD loop of PKD1 interact directly with AAV5, whereas residues in strands B/C/E and the BC loop of PKD2 make contact with AAV1. These findings further the understanding of the distinct mechanisms by which AAVR recognizes various AAV serotypes and provide an example of a single receptor engaging multiple viral serotypes with divergent rules.