Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase.
Acta Crystallogr D Biol Crystallogr
; 59(Pt 5): 940-2, 2003 May.
Article
em En
| MEDLINE
| ID: mdl-12777818
ABSTRACT
Collagen prolyl 4-hydroxylases catalyze the hydroxylation of -X-Pro-Gly- sequences and play an essential role in the synthesis of all collagens. They require Fe(2+), 2-oxoglutarate, molecular oxygen and ascorbate, and all vertebrate collagen prolyl 4-hydroxylases are alpha(2)beta(2) tetramers. The alpha-subunits contain separate catalytic and peptide substrate-binding domains. Here, the crystallization of the peptide substrate-binding domain consisting of residues 144-244 of the 517-residue human alpha(I) subunit is described. The crystals are well ordered and diffract to at least 3 A. The space group is P3(1) or P3(2) and the asymmetric unit most probably contains a dimer.
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Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Prolina
/
Pró-Colágeno-Prolina Dioxigenase
/
Colágeno Tipo I
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Finlândia