The structure of a synthetic pepsin inhibitor complexed with endothiapepsin

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Cooper, Jon, Foundling, Steve, Hemmings, Andrew, Blundell, Tom, Jones, D. Michael, Hallett, Allan and Szelke, Michael (1987) The structure of a synthetic pepsin inhibitor complexed with endothiapepsin. European Journal of Biochemistry, 169 (1). pp. 215-221. ISSN 0014-2956

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Abstract

The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X‐ray diffraction at 0.20‐nm resolution and refined to an agreement factor of 0.20. The inhibitor: (Formula Presented.) is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in place of the scissile bond, a reduced peptide group which is resistant to hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in an extended conformation with the reduced bond close to the essential aspartate side‐chains of the enzyme. The hydrogen bonds and hydrophobic interactions between the enzyme and the inhibitor do not induce large conformational changes.

Item Type:	Article
Uncontrolled Keywords:	biochemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	13 Feb 2025 12:30
Last Modified:	16 Feb 2025 06:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/98463
DOI:	10.1111/j.1432-1033.1987.tb13600.x

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