Structure of human ADAM-8 catalytic domain complexed with batimastat.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 6): 616-21, 2012 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-22684055
ABSTRACT
The role of ADAM-8 in cancer and inflammatory diseases such as allergy, arthritis and asthma makes it an attractive target for drug development. Therefore, the catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme-inhibitor complex was refined to 2.1 Å resolution. ADAM-8 has an overall fold similar to those of other ADAM members, including a central five-stranded ß-sheet and a catalytic Zn(2+) ion. However, unique differences within the S1' binding loop of ADAM-8 are observed which might be exploited to confer specificity and selectivity to ADAM-8 competitive inhibitors for the treatment of diseases involving this enzyme.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fenilalanina
/
Inibidores de Proteases
/
Tiofenos
/
Domínio Catalítico
/
Proteínas ADAM
/
Proteínas de Membrana
Limite:
Humans
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article