Proline provides site-specific flexibility for in vivo collagen

Scientific Reports
Wing Ying ChowMelinda J Duer

Abstract

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.

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Citations

Oct 2, 2019·Angewandte Chemie·Shehrazade JekhmaneMarkus Weingarth
Jul 28, 2019·Essays in Biochemistry·Pekka RappuJyrki Heino
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Jan 18, 2022·Clinical & Experimental Ophthalmology·Kate E Keller, Donna M Peters

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Methods Mentioned

BETA
NMR
X-ray

Software Mentioned

Avogadro
MUSCLE

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