Molecular Structure of an Aspartic Proteinase Aymogen, Porcine Pepsinogen, at 1.8 A Resolution

The only well-understood mechanism of zymogen activation is that of the serine proteinases, in which proteolytic cleavage leads to conformational changes resulting in a functional active site. A different mechanism is now unveiled by the crystal structure of pepsinogen. Salt bridges that stabilize t...

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Bibliographic Details
Published in:Nature (London) 1986-01, Vol.319 (6048), p.33-33
Main Authors: James, Michael N G, Sielecki, Anita R
Format: Article
Language:English
Subjects:
Minerals
Science
Online Access:Get full text
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Summary:The only well-understood mechanism of zymogen activation is that of the serine proteinases, in which proteolytic cleavage leads to conformational changes resulting in a functional active site. A different mechanism is now unveiled by the crystal structure of pepsinogen. Salt bridges that stabilize the positioning of the N-terminal proenzyme segment across the active site of pepsin are disrupted at low pH, releasing the amino-terminal segment and thereby exposing the catalytic apparatus and the substrate-binding sites.
ISSN:0028-0836
1476-4687