Eur J Biochem. 1987 Nov 16;169(1):215-21.

The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.

Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M.

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Department of Crystallography, Birkbeck College, London, England.

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: Pro Thr Glu Phe-R-Phe Arg Glu (R = -CH2NH-) 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.

PMID:: 3119339; [PubMed - indexed for MEDLINE]

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Cited by 7 PubMed Central articles

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Structures reported by this article

The Structure Of A Synthetic Pepsin Inhibitor Complexed With Endothiapepsin

PDB: 2ER6

Source: Cryphonectria parasitica, synthetic construct

Method: X-Ray Diffraction

Resolution: 2 Å

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The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
Eur J Biochem. 1987 Nov 16 ;169(1):215-21.

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