[The structure of pepsin. I. Molecular self-symmetry of the enzyme and implications for the evolution of aspartate proteinases].
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.
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000235:genetics; D005796:Genes; D008958:Models, Molecular; D010434:Pepsin A / Q000235:genetics; D010455:Peptides; D011487:Protein Conformation
D010455:Peptides; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A
Struktura pepsina. I. Sobstvennaia simmetriia molekuly fermenta i vozmozhnye puti évoliutsii aspartatnykh proteinaz.