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1.
FIG. 2.

FIG. 2. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

The crystal structure of Fab 14 is shown in stereo as a ribbon diagram. The CDRs are labeled for the heavy chain (cyan) and the light chain (magenta).

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
2.
FIG. 7.

FIG. 7. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

The Fab footprints for the A site (red X's) and the B site (blue X's) overlap with the TfR binding site, identified in black by amino acid number (19). The antibodies 8, 15, and 16 directed to the B site show the greatest amount of overlap with the receptor binding site.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
3.
FIG. 4.

FIG. 4. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

Amino acid sequences of the light and heavy chains aligned according to consensus sequences (red) and CDR loops (blue). Residues in contact with the viral surface are indicated by asterisks. Since only the light chain sequence was determined for Fab 16, the mouse antibody 1AIF Fab was used to interpret the Fab 16 density.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
4.
FIG. 3.

FIG. 3. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

Surface-rendered cryoEM reconstructions of virus complexed with each of eight fragments from neutralizing antibodies described by Nelson et al. (35). Surfaces are shown at one sigma of the cryoEM density. Density further than a 125-Å radius from the center of the virus is shown in gray. Shown directly below each reconstruction is the footprint of the Fab in the complex. Both complexes and footprints are color coded red for antibodies directed to the A site and blue for antibodies directed to the B site.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
5.
FIG. 6.

FIG. 6. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

Capsid protein of CPV viewed approximately tangentially to the surface of the virus, showing the closest icosahedral five- and threefold symmetry axes. Spheres show the positions of residues previously identified as belonging to the A site (red) and B site (blue). Additional residues found in the footprints of all antibodies directed to the A site are shown in magenta, and residues common to all B site antibodies are shown in cyan. Secondary structural elements, or β strands, are labeled A to I.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
6.
FIG. 8.

FIG. 8. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

The cryoEM density of the CPV-Fab 14 complex shown as a surface-contoured mesh in a slab view at the region of the threefold spike. The icosahedral threefold axis is indicated by a dark gray axis. The heavy chain (green) and the light chain (gold) of Fab 14 are fitted into the Fab density. Both CPV (blue) and FPV (magenta) have been fitted into the viral density to show the very subtle differences between the two viruses at loops 1 and 2 in the interface of the capsid interactions with the Fab.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
7.
FIG. 5.

FIG. 5. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

The viral surface is shown as a stereographic projection where the polar angles φ and θ represent the latitude and longitude of a point on the viral surface, respectively (63). (A) The residues shared by the Fab footprints are defined as the common A site and common B site and outlined in red and blue, respectively. (B) All of the residues within the antibody footprints define a total antigenic surface outlined in black. The viral surface residues are colored according to the distance from the center of the virus, with red amino acids being the furthest away and blue representing depressions in the viral surface.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.
8.
FIG. 1.

FIG. 1. From: Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids .

The viral surface is shown as a stereographic projection where the polar angles φ and θ represent the latitude and longitude of a point on the viral surface, respectively (63). The virus surface is represented as a quilt of amino acids (52), and the icosahedral asymmetric unit of the virus is indicated by the triangular boundary. To visualize the different copies of the capsid protein in the road map that comprise the asymmetric unit, VP2 molecules are displayed in tints of magenta, green, and blue. Escape mutations from neutralizing antibodies are colored red for site A and dark blue for site B.

Susan Hafenstein, et al. J Virol. 2009 June;83(11):5556-5566.

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