1VU0: Structure-function Analysis of Receptor-binding in Adeno-associated Virus Serotype 6 (Aav-6)

Citation:
Abstract
Crystal structures of the AAV-6 capsid at 3A reveal a subunit fold homologous to other parvoviruses with greatest differences in two external loops. The electrostatic potential suggests that receptor-attachment is mediated by four residues: Arg(576), Lys(493), Lys(459) and Lys(531), defining a positively charged region curving up from the valley between adjacent spikes. It overlaps only partially with the receptor-binding site of AAV-2, and the residues endowing the electrostatic character are not homologous. Mutational substitution of each residue decreases heparin affinity, particularly Lys(531) and Lys(459). Neither is conserved among heparin-binding serotypes, indicating that diverse modes of receptor attachment have been selected in different serotypes. Surface topology and charge are also distinct at the shoulder of the spike, where linear epitopes for AAV-2's neutralizing monoclonal antibody A20 come together. Evolutionarily, selection of changed side-chain charge may have offered a conservative means to evade immune neutralization while preserving other essential functionality.
MMDB ID: 99554
PDB Deposition Date: 2011/9/13
Updated in MMDB: 2012/08 
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Merged PDB IDs:1VU0 1VU1 3TSX
Asymmetric Unit for 1VU0: 60-meric
Molecular Components in 1VU0
Label Count Molecule
Proteins (60 molecules)
60
Capsid Protein VP1
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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