Table 3 Solvent accessible surface area of Tyr79 of wheat, peach and barley LTPs.

From: Ligand binding to an Allergenic Lipid Transfer Protein Enhances Conformational Flexibility resulting in an Increase in Susceptibility to Gastroduodenal Proteolysis

LTP

Unliganded (Å 2 )

1 ligand (Å 2 ) bound

2 ligands (Å 2 ) bound

Wheat

5 (1GH1)

38 (1CZ2)

83 (1BWO)

Peach

22 (2ALG mol B) ϑ

—

52 (2ALG mol A)

  1. Surface area values are averaged over the fifteen, twelve and four ensemble models of the 1GH1, 1CZ2 and 1LIP NMR structures, respectively. For the crystal structures, values are averaged over the two molecules present in each of the asymmetric units of 3GSH and 1BWO (the asymmetric unit of 1MID contains a single LTP molecule). PDB accession codes are in parenthesis.
  2. ϑMolecule B present in the asymmetric unit of the peach LTP crystal structure 2ALG was observed to bind a single lauric acid molecule in an unconventional manner, with the ligand only partially occupying the cavity (Fig. 4D). Therefore, for the purposes of this study, the LTP molecule is regarded as “unliganded”.
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