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Proline provides site-specific flexibility for in vivo collagen

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. and Duer, Melinda J. 2018. Proline provides site-specific flexibility for in vivo collagen. Scientific Reports 8 (1) , 13809. 10.1038/s41598-018-31937-x

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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 13C-13C correlation NMR spectroscopy on 13C-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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Publisher: Nature Publishing Group
ISSN: 2045-2322
Date of First Compliant Deposit: 19 September 2018
Date of Acceptance: 24 August 2018
Last Modified: 20 Sep 2018 14:41

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