Andreeva N S
Mol Biol (Mosk). 1985 Jan-Feb;19(1):218-24.
This is the first paper in the series of publications on the detailed description of different aspects of pepsin structure. It concerns the domain structure of the enzyme and the topology of the arrangement of beta-strands in pepsin and related aspartic proteases, this topology being quite different from that of all other beta-proteins. The topology, molecular symmetry and the close proximity of the N- and C-termini of domains suggest that at the first stages of evolution polypeptide chains of some preproteins could be closed in rings, which become open at the subsequent stages. Their genes duplicated twice, and the fusion process resulted in a gene consisting of similar parts.
这是关于胃蛋白酶结构不同方面详细描述的系列出版物中的第一篇论文。它涉及该酶的结构域结构以及胃蛋白酶和相关天冬氨酸蛋白酶中β链排列的拓扑结构，这种拓扑结构与所有其他β蛋白的拓扑结构有很大不同。结构域的拓扑结构、分子对称性以及N端和C端的紧密接近表明，在进化的最初阶段，一些前体蛋白的多肽链可能会形成环状结构，而在随后的阶段这些环会打开。它们的基因进行了两次复制，融合过程产生了一个由相似部分组成的基因。
