The plasticity of the ß-trefoil fold constitutes an evolutionary platform for protease inhibition.
J Biol Chem
; 286(51): 43726-43734, 2011 Dec 23.
Article
em En
| MEDLINE
| ID: mdl-22027836
ABSTRACT
Proteases carry out a number of crucial functions inside and outside the cell. To protect the cells against the potentially lethal activities of these enzymes, specific inhibitors are produced to tightly regulate the protease activity. Independent reports suggest that the Kunitz-soybean trypsin inhibitor (STI) family has the potential to inhibit proteases with different specificities. In this study, we use a combination of biophysical methods to define the structural basis of the interaction of papaya protease inhibitor (PPI) with serine proteases. We show that PPI is a multiple-headed inhibitor; a single PPI molecule can bind two trypsin units at the same time. Based on sequence and structural analysis, we hypothesize that the inherent plasticity of the ß-trefoil fold is paramount in the functional evolution of this family toward multiple protease inhibition.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeo Hidrolases
/
Inibidores de Proteases
/
Inibidores Enzimáticos
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Bélgica