Structural aspects of hydroxyproline-containing proteins

Journal of Biomolecular Structure & Dynamics
V S Ananthanarayanan

Abstract

The occurrence of hydroxyproline (Hyp) in collagen, C1q and acetylcholineesterase (AChE) raises important questions concerning the role of this unusual imino acid in the structure and function of these proteins. Available data on collagen indicate that Hyp is necessary for the normal secretion of the protein after its synthesis and for the integrity of the triple-helical conformation. Studies from our laboratory have dealt with the structural aspects of the posttranslational conversion of proline to hydroxyproline in collagen mediated by prolyl hydroxylase. We proposed that the beta-turn conformation at the Pro-Gly segments in the nascent procollagen molecule are the sites of the enzymatic hydroxylation and that this conformation changes over to the collagen-like helix as a result of the hydroxylation process. Recently, we have provided additional experimental support to our proposal by a) synthesizing specific beta-turn oligopeptides containing the Pro-Gly as well as Pro-Ala and Pro-DAla sequences and showing that these act as inhibitors of the enzymatic hydroxylation of a synthetic substrate and b) demonstrating, by circular dichroism spectroscopy, the occurrence of a conformational change leading to the triple-helix as a dir...Continue Reading

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Citations

Dec 1, 1993·Journal of Biomolecular Structure & Dynamics·B S Zhorov, V S Ananthanarayanan
Mar 15, 2020·Metabolomics : Official Journal of the Metabolomic Society·Moamen M ElmassryAbdul N Hamood
Apr 23, 2021·Microbial Cell Factories·Zhenyu ZhangXiaohe Chu

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