7QIT

CRYSTAL STRUCTURE OF THE P1 trifluoroethylglycine (TfeGly) BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

7QIT の概要

• エントリーDOI: 10.2210/pdb7qit/pdb
• 関連するPDBエントリー: 7QIQ 7QIR 7QIS
• 分子名称: Chymotrypsin A chain A, Chymotrypsin A chain B, Chymotrypsin A chain C, ... (7 entities in total)
• 機能のキーワード: chymotrypsin, serine proteinase, bovine pancreatic trypsin inhibitor, bpti, protein-protein interaction, s1 pocket, primary specificity, hydrolase-hydrolase inhibitor complex, hydrolase
• 由来する生物種: Bos taurus (cattle); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 68284.13

構造登録者

Dimos, N.,Leppkes, J.,Koksch, B.,Wahl, M.C.,Loll, B. (登録日: 2021-12-15, 公開日: 2022-03-09, 最終更新日: 2024-11-13)

主引用文献

Leppkes, J.,Dimos, N.,Loll, B.,Hohmann, T.,Dyrks, M.,Wieseke, A.,Keller, B.G.,Koksch, B.
Fluorine-induced polarity increases inhibitory activity of BPTI towards chymotrypsin.
Rsc Chem Biol, 3:773-782, 2022

PubMed Abstract: Substituting the P position in bovine pancreatic trypsin inhibitor (BPTI) is known to heavily influence its inhibitory activity towards serine proteases. Side-chain fluorinated aliphatic amino acids have been shown to alter numerous properties of peptides and proteins and thus are of interest in the context of BPTI. In our study, we systematically investigated the site-specific incorporation of non-canonical amino acids into BPTI by microwave-assisted solid-phase peptide synthesis (SPPS). Inhibitor activity of the variants was tested towards the serine protease α-chymotrypsin. We observed enhanced inhibition of two fluorinated BPTIs compared to wild type and hydrocarbon variants. To further investigate the complexes, we performed X-ray structure analysis. Our findings underline the power fluorine offers as a tool in protein engineering to beneficially alter the effects on phenomena as protein-protein interactions.

PubMed: 35755190
DOI: 10.1039/d2cb00018k

実験手法

X-RAY DIFFRACTION (1.99 Å)