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Review
. 2009 Nov;5(11):e1000481.
doi: 10.1371/journal.ppat.1000481. Epub 2009 Nov 26.

Immunoglobulin superfamily virus receptors and the evolution of adaptive immunity

Terence S Dermody  1 , Eva Kirchner, Kristen M Guglielmi, Thilo Stehle
Affiliations
Review

Immunoglobulin superfamily virus receptors and the evolution of adaptive immunity

Terence S Dermody et al. PLoS Pathog. 2009 Nov.
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. Contact areas in Fab and virus receptors.
(A) Ribbon drawing of mFab 231 (left) (; 1IGT) and the extracellular domains of hJAM-A (right) (; 1NBQ). Variable (V) and constant (C) domains of heavy (H) and light (L) chains and D1 and D2 domains of JAM-A are labeled. (B) Ribbon drawing of the variable domain of the light chain (VL) of the mFab shown in (A). CDRs are colored green. (C–E) Ribbon drawings of the complexed D1 domains of (C) CD4 (; 1GC1), (D) hJAM-A (; 3EOY), and (E) CAR (; 1KAC). Residues contacting the virus proteins with a distance cutoff of 4 Å are colored green. (F) Structural alignment of mFab 231 VL (; 1IGT), CD4 D1 (; 1CDJ), hJAM-A D1 (; 1NBQ), and CAR D1 (; 1EAJ) performed using MODELLER (program Web site: http://salilab.org/modeller/). β-strands are indicated, and conserved residues are highlighted in grey. mFab 231 VL CDRs and residues in CD4, hJAM-A, and CAR that contact the viral attachment proteins gp120, σ1, and fiber, respectively, with a distance cutoff of 4 Å, are highlighted in green.
See this image and copyright information in PMC

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