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. Author manuscript; available in PMC: 2010 Jun 1.
Published in final edited form as: Gene Ther. 2009 Dec;16(12):1416–1428. doi: 10.1038/gt.2009.101

Figure 3. Structure-function correlates of singleton modification on vector phenotype.

Figure 3

Singleton residues locations from categories I, II, and IV–VII are mapped onto the X-ray crystal structure model of AAV8. Numbers and typesetting refer to AAV8 VP1 residue 220 – 738 of singleton locations of the categories defined in Table 4. For I, II, V and VII, the panels on the left show the outer surfaces of the viral capsid (external) and those on the right show 180° rotated views of the same representation showing the inner surface (internal). An internal view only is provided for IV and VI. The surface representation of the reference VP monomer is shown in yellow, and the backbones of symmetry related VP monomers are shown in cyan, orange, green and aqua for VP monomers that are 5-fold related (labeled 5f), magenta and violet for 3-fold related (3f), and pink for the 2-fold related (2f), respectively. The mutated residues are colored blue (for residues that show a phenotype) or cyan (residues in parenthesis in Fig. 2A with no phenotype). The location of a 5-fold axis is shown as a black pentagon.