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.Crystal structure of the lectin domain of chick polyclonal anti-bromelain IgY: a recognition site for bromelain inhibitors.
The lectin domain of chick polyclonal anti-bromelain IgY is a modular protein (32KDa) with both lectin activity and enzymatic protease inhibitory properties. A recombinant alpha-helical peptide carrying both properties (VLDPGYPGVVTGPQGR) was synthesized to demonstrate a direct correlation between inhibitory properties and the presence of the helical conformation. Crystallization trials were unsuccessful and subunit recombination promoted the formation of a dimer instead of the expected tetramer. The structure of this dimeric lectin domain was therefore solved and refined to 2.5A resolution. The overall fold of the protein reveals a homodimer composed of two 32KDa polypeptide chains, linked by their VL domain at their C termini. The central three residues of the newly produced VLDPGYPGVVTGPQGR peptide, together with the flanking peptide, undergo a helical turn to stabilize the tetramer of anti-bromelain IgY.{N}}(1_{\left\{ v \leq z \right\}}, 1_{\left\{ u \leq z \right\}}) \left( {{\mathcal{L}}^{{\mathbb{P}}_Y}}(1_{\left\{ v \leq z \right\}}, 1_{\left\{
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