Liepina I, Nikiforovich G V, Paiva A C
Biochem Biophys Res Commun. 1984 Jul 31;122(2):700-5. doi: 10.1016/s0006-291x(84)80090-x.
Linear and cyclic peptides containing the His6-Pro7-Phe8-His9 sequence of renin's substrate (angiotensinogen) have been shown to be effective competitive inhibitors of the enzyme. Calculations and comparison of low energy structures for these peptides give support to the existence of a beta-turn-like structure involving the His-Pro-Phe-His region of the renin substrate and of the competitive inhibitors containing that sequence. This structure may be regarded as a possible "inhibition conformation", occurring in the process of binding to renin.
含有肾素底物(血管紧张素原)的His6 - Pro7 - Phe8 - His9序列的线性和环状肽已被证明是该酶的有效竞争性抑制剂。对这些肽的低能结构进行计算和比较,支持了肾素底物以及含有该序列的竞争性抑制剂中存在一个涉及His - Pro - Phe - His区域的类β - 转角结构。这种结构可被视为在与肾素结合过程中可能出现的“抑制构象”。