5XW9

Crystal Structure of Porcine pancreatic trypsin with tripeptide inhibitor, PRY, at pH 7

5XW9 の概要

• エントリーDOI: 10.2210/pdb5xw9/pdb
• 分子名称: Trypsin, Acetylated-Pro-Arg-Tyr Inhibitor, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: protease, inhibitor, complex, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Sus scrofa (Pig); 詳細
• 細胞内の位置: Secreted, extracellular space: P00761 P00761
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 24948.02

構造登録者

Saikhedkar, N.S.,Bhoite, A.S.,Giri, A.P.,Kulkarni, K.A. (登録日: 2017-06-29, 公開日: 2018-03-28, 最終更新日: 2024-10-30)

主引用文献

Saikhedkar, N.S.,Joshi, R.S.,Bhoite, A.S.,Mohandasan, R.,Yadav, A.K.,Fernandes, M.,Kulkarni, K.A.,Giri, A.P.
Tripeptides derived from reactive centre loop of potato type II protease inhibitors preferentially inhibit midgut proteases of Helicoverpa armigera.
Insect Biochem. Mol. Biol., 95:17-25, 2018

PubMed Abstract: Potato type II protease inhibitors (Pin-II PIs) impede the growth of lepidopteran insects by inhibiting serine protease-like enzymes in the larval gut. The three amino acid reactive centre loop (RCL) of these proteinaceous inhibitors is crucial for protease binding and is conserved across the Pin-II family. However, the molecular mechanism and inhibitory potential of the RCL tripeptides in isolation of the native protein has remained elusive. In this study, six peptides corresponding to the RCLs of the predominant Pin-II PIs were identified, synthesized and evaluated for in vitro and in vivo inhibitory activity against serine proteases of the polyphagous insect, Helicoverpa armigera. RCL peptides with sequences PRN, PRY and TRE were found to be potent inhibitors that adversely affected the growth and development of H. armigera. The binding mechanism and differential affinity of the RCL peptides with serine proteases was delineated by crystal structures of complexes of the RCL peptides with trypsin. Residues P1 and P2 of the inhibitors play a crucial role in the interaction and specificity of these inhibitors. Important features of RCL peptides like higher inhibition of insect proteases, enhanced efficacy at alkaline gut pH, longer retention and high stability in insect gut make them suitable molecules for the development of sustainable pest management strategies for crop protection.

PubMed: 29486250
DOI: 10.1016/j.ibmb.2018.02.001

実験手法

X-RAY DIFFRACTION (2 Å)