2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor.
Biochemistry
; 42(22): 6709-18, 2003 Jun 10.
Article
em En
| MEDLINE
| ID: mdl-12779325
ABSTRACT
This paper reports the first structure of a member of the Kex2/furin family of eukaryotic pro-protein processing proteases, which cleave sites consisting of pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar in its global fold to the subtilisin-like superfamily of degradative proteases. Analysis of the complex provides a structural basis for the extreme selectivity of this enzyme family that has evolved from a nonspecific subtilisin-like ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of nine beta strands and may potentially be involved, along with the buried Ca(2+) ion, in creating the highly determined binding site for P(1) arginine.
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Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Inibidores de Proteases
/
Ácidos Borônicos
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Subtilisinas
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Proteínas de Saccharomyces cerevisiae
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Pró-Proteína Convertases
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article