Inhibitor Binding Induces Structural Changes in Porcine Pepsin
- 1 January 1991
- book chapter
- Published by Springer Science and Business Media LLC in Advances in experimental medicine and biology
- Vol. 306, 9-21
- https://doi.org/10.1007/978-1-4684-6012-4_2
Abstract
Crystal structures of several fungal aspartic proteinases have been refined at high resolution: penicillopepsin1, Endothia parasitica pepsin2 and Rhizopus chinensis protease.3 The structure of a recombinant form of human renin has been solved4 at 2.5 Å and the refined structures of two other mammalian aspartic proteinases have been reported recently: chymosin at 2.3 Å resolution5, and the monoclinic form of porcine pepsin at 2.3 and 1.8 Å resolution6,7, as well as the original hexagonal crystal form8.Keywords
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