期刊
SCIENTIFIC REPORTS
卷 8, 期 -, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41598-018-31937-x
关键词
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资金
- BBSRC [BB/GO21329/1]
- EPSRC
- British Heart Foundation [RG/09/003/27122, PG/08/011/24416]
- Wellcome Trust [094470/Z/10/Z]
- ERC
- Raymond and Beverly Sackler Fund for Physics of Medicine, University of Cambridge
- EPSRC [EP/N035003/1] Funding Source: UKRI
- Wellcome Trust [094470/Z/10/Z] Funding Source: Wellcome Trust
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-13-C-13 correlation NMR spectroscopy on C-13-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.
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