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Solution Structure of a Repeated Unit of the ABA-1 Nematode Polyprotein Allergen of Ascaris Reveals a Novel Fold and Two Discrete Lipid-Binding Sites

Figure 3

The nuclear magnetic resonance structure of ABA-1A in solution.

(A) A stereo plot (wall-eyed) depicting the 20 lowest energy structures (from a total of 100) superimposed on the backbone heavy atoms of residues 4–126. (B, C, D) Three cartoon views (A and E rotated 180° about the y-axis and 90° about the x-axis with respect to (B) of the representative structure of ABA-1A with a color progression from blue (N-terminus) to red (C-terminus). (C) Enlargements of the wide helical turn at the end of α-helix A (upper inset) and the local environment of the absolutely conserved position Trp15 of NPAs (lower inset). Figures prepared using PyMol.

Figure 3

doi: https://doi.org/10.1371/journal.pntd.0001040.g003