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The three-dimensional structure of the papain-leupeptin complex has been determined by X-ray crystallography to a resolution of 2.1 A (overall R-factor = 19.8%). The structure indicates that: (i) leupeptin contacts the S subsites of the papain active site and not the S' subsites; (ii) the 'carbonyl' carbon atom of the inhibitor is covalently bound by the Cys-25 sulphur atom of papain and is tetrahedrally coordinated; (iii) the 'carbonyl' oxygen atom of the inhibitor faces the oxyanion hole and makes hydrogen bond contacts with Gln-19 and Cys-25.

Original publication

DOI

10.1016/0014-5793(93)81128-m

Type

Journal article

Journal

FEBS Lett

Publication Date

02/01/1993

Volume

315

Pages

38 - 42

Keywords

Amino Acid Sequence, Binding Sites, Crystallography, In Vitro Techniques, Leupeptins, Models, Molecular, Molecular Sequence Data, Papain, Protein Structure, Tertiary, X-Ray Diffraction