Structure of a Kunitz-type potato cathepsin D inhibitor.
J Struct Biol
; 192(3): 554-560, 2015 Dec.
Article
em En
| MEDLINE
| ID: mdl-26542926
ABSTRACT
Potato cathepsin D inhibitor (PDI) is a glycoprotein of 188 amino acids which can inhibit both the aspartic protease cathepsin D and the serine protease trypsin. Here we report the first X-ray structure of PDI at a resolution of 2.1 Å showing that PDI adopts a ß-trefoil fold, which is typical of the Kunitz-family protease inhibitors, with the inhibitory loops protruding from the core. Possible reactive-site loops including one involving a unique disulphide and another involving a protruding 310 helix are identified and docking studies indicate the mode of action of this unusual bi-functional inhibitor.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
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Catepsina D
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Domínio Catalítico
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article