Details

Autor(en) / Beteiligte

• Chow, Wing Ying
• Forman, Chris J
• Bihan, Dominique
• Puszkarska, Anna M
• Rajan, Rakesh
• Reid, David G
• Slatter, David A
• Colwell, Lucy J
• Wales, David J
• Farndale, Richard W
• Duer, Melinda J

Titel

Proline provides site-specific flexibility for in vivo collagen

Ist Teil von

• Scientific reports, 2018-09, Vol.8 (1), p.13809-13, Article 13809

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2018

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Fibrillar collagens have mechanical and biological roles, providing tissues with both tensile strength and cell binding sites which allow molecular interactions with cell-surface receptors such as integrins. A key question is: how do collagens allow tissue flexibility whilst maintaining well-defined ligand binding sites? Here we show that proline residues in collagen glycine-proline-hydroxyproline (Gly-Pro-Hyp) triplets provide local conformational flexibility, which in turn confers well-defined, low energy molecular compression-extension and bending, by employing two-dimensional C- C correlation NMR spectroscopy on C-labelled intact ex vivo bone and in vitro osteoblast extracellular matrix. We also find that the positions of Gly-Pro-Hyp triplets are highly conserved between animal species, and are spatially clustered in the currently-accepted model of molecular ordering in collagen type I fibrils. We propose that the Gly-Pro-Hyp triplets in fibrillar collagens provide fibril "expansion joints" to maintain molecular ordering within the fibril, thereby preserving the structural integrity of ligand binding sites.