Wong C H, Lee T J, Lee T Y, Lu T H, Yang I H
Biochemistry. 1979 Apr 17;18(8):1638-40. doi: 10.1021/bi00575a041.
The structure of acid protease from Endothia parasitica in strongly cross-linked form is compared with that of the untreated protein at 2.45-a resolution. The only observed conformation change introduced by the cross-linking reaction is at the N terminal. Otherwise the two main chain structures are essentially identical. Approximately 2 molecules of the inhibitor, 1,2-epoxy-3-(p-nitrophenoxy)propane, are found to be incorporated into each protein molecule. They are covalently bound to the two aspartic residues at the active center.
将来自寄生内座壳菌的强交联形式的酸性蛋白酶结构与未经处理的蛋白质在2.45埃分辨率下的结构进行比较。交联反应引入的唯一观察到的构象变化发生在N端。否则，两条主链结构基本相同。发现每个蛋白质分子中约有2个抑制剂分子，即1,2-环氧-3-(对硝基苯氧基)丙烷掺入。它们共价结合到活性中心的两个天冬氨酸残基上。
