The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens.

doi:10.1007/s00726-008-0073-2

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Article

The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens.

Amino acids - 1 Nov 2008

Krane Stephen M

Abstract excerpt

Collagens are among proteins that undergo several post-translational modifications, such as prolyl hydroxylation, that occur during elongation of the nascent chains in the endoplasmic reticulum. The major structural collagens, types I, II and III, have large, uninterrupted triple helices, comprising three polyproline II-like chains supercoiled around a common axis. The structure has a requirement for glycine, as...

Topics

Amino Acid Sequence
Animals
Collagen
Glycine
Humans
Hydroxyproline
Mice
Models, Biological
Models, Genetic
Molecular Sequence Data
Mutation
Osteogenesis Imperfecta
Proline
Proteins

Source

Open in PubMed

Identifiers

PMID: 18431533
DOI: 10.1007/s00726-008-0073-2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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