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Updated: Aug 7, 2026

An Improved Method for the Preparation of Type I Collagen From Skin
Published on: January 22, 2014
Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase
Mira Pekkala1, Reija Hieta, Petri Kursula
1Biocenter Oulu and Department of Biochemistry, University of Oulu, PO Box 3000, FIN-90014, Finland.
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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