1BTY

Crystal structure of beta-trypsin in complex with benzamidine

1BTY の概要

• エントリーDOI: 10.2210/pdb1bty/pdb
• 分子名称: BETA-TRYPSIN, CALCIUM ION, BENZAMIDINE, ... (4 entities in total)
• 機能のキーワード: benzamidine inhibited, hydrolase (serine proteinase), hydrolase
• 由来する生物種: Bos taurus (BOVINE)
• 細胞内の位置: Secreted, extracellular space: P00760
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24173.18

構造登録者

Stroud, R.M.,Katz, B.A.,Finer-Moore, J. (登録日: 1995-05-17, 公開日: 1995-10-15, 最終更新日: 2024-11-13)

主引用文献

Katz, B.A.,Finer-Moore, J.,Mortezaei, R.,Rich, D.H.,Stroud, R.M.
Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.
Biochemistry, 34:8264-8280, 1995

PubMed Abstract: A novel class of mechanism-based inhibitors of the serine proteases is developed using epitaxial selection. Tripeptide boronates esterified by an alcohol or alcohols at the boron retain the tight binding to trypsin-like enzymes associated with transition-state analogs and incorporate additional groups that can be utilized for selectivity between proteases. Formed by reaction of a series of alcohols with the inhibitor boronate oxygen(s), the most structurally compatible alcohol-derivatized inhibitors are either selected by binding to the enzyme (epitaxial selection) or assembled by epitaxial reaction on the enzyme surface. Mass spectrometry of the derivatized boronates and X-ray crystallography of the complexes identify the chemical structures and the three-dimensional interactions of inhibitors generated. This scheme also engineers novel, potent (Ki approximately 7 nM), and more specific inhibitors of individual serine proteases, by derivitizations of compounds obtained by epitaxial selection.

PubMed: 7599119
DOI: 10.1021/bi00026a008

実験手法

X-RAY DIFFRACTION (1.5 Å)