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. 1979 Oct;76(10):5119–5123. doi: 10.1073/pnas.76.10.5119

Beta-turns in nascent procollagen are sites of posttranslational enzymatic hydroxylation of proline.

S K Brahmachari, V S Ananthanarayanan
PMCID: PMC413091  PMID: 228279

Abstract

The selective hydroxylation of proline residues in nascent procollagen chains by prolyl hydroxylase (EC 1.14.11.2) can be understood in terms of the conformational feature of the -Pro-Gly-segments in linear peptides and globular proteins. The folded beta-turn conformation in such segments appears to be the conformational requirement for proline hydroxylation. The available data on the hydroxylation of native and synthetic substrates of prolyl hydroxylase are explained on the basis of the extent of beta-turn formation in them. Taken in conjunction with the conformational features of the hydroxyproline residue, our results bring out the conformational reason for the posttranslational proline hydroxylation which, it is proposed, leads to the "straightening" of the beta-turn segments into the linear triple-helical conformation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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