Proline provides site-specific flexibility for in vivo collagen

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 wel...

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Autores principales:	Wing Ying Chow, Chris J. Forman, Dominique Bihan, Anna M. Puszkarska, Rakesh Rajan, David G. Reid, David A. Slatter, Lucy J. Colwell, David J. Wales, Richard W. Farndale, Melinda J. Duer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	13Cγ Chemical Shifts Proline Ring Collagen Model Peptides Collagen Triple Helix Backbone Dihedrals Medicine R Science Q
Acceso en línea:	https://doaj.org/article/eb22423885e3428eb990590955b04686
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spelling	oai:doaj.org-article:eb22423885e3428eb990590955b046862021-12-02T15:08:41ZProline provides site-specific flexibility for in vivo collagen10.1038/s41598-018-31937-x2045-2322https://doaj.org/article/eb22423885e3428eb990590955b046862018-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-31937-xhttps://doaj.org/toc/2045-2322Abstract 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.Wing Ying ChowChris J. FormanDominique BihanAnna M. PuszkarskaRakesh RajanDavid G. ReidDavid A. SlatterLucy J. ColwellDavid J. WalesRichard W. FarndaleMelinda J. DuerNature Portfolioarticle13Cγ Chemical ShiftsProline RingCollagen Model PeptidesCollagen Triple HelixBackbone DihedralsMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	13Cγ Chemical Shifts Proline Ring Collagen Model Peptides Collagen Triple Helix Backbone Dihedrals Medicine R Science Q
spellingShingle	13Cγ Chemical Shifts Proline Ring Collagen Model Peptides Collagen Triple Helix Backbone Dihedrals Medicine R Science Q Wing Ying Chow Chris J. Forman Dominique Bihan Anna M. Puszkarska Rakesh Rajan David G. Reid David A. Slatter Lucy J. Colwell David J. Wales Richard W. Farndale Melinda J. Duer Proline provides site-specific flexibility for in vivo collagen
description	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.
format	article
author	Wing Ying Chow Chris J. Forman Dominique Bihan Anna M. Puszkarska Rakesh Rajan David G. Reid David A. Slatter Lucy J. Colwell David J. Wales Richard W. Farndale Melinda J. Duer
author_facet	Wing Ying Chow Chris J. Forman Dominique Bihan Anna M. Puszkarska Rakesh Rajan David G. Reid David A. Slatter Lucy J. Colwell David J. Wales Richard W. Farndale Melinda J. Duer
author_sort	Wing Ying Chow
title	Proline provides site-specific flexibility for in vivo collagen
title_short	Proline provides site-specific flexibility for in vivo collagen
title_full	Proline provides site-specific flexibility for in vivo collagen
title_fullStr	Proline provides site-specific flexibility for in vivo collagen
title_full_unstemmed	Proline provides site-specific flexibility for in vivo collagen
title_sort	proline provides site-specific flexibility for in vivo collagen
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/eb22423885e3428eb990590955b04686
work_keys_str_mv	AT wingyingchow prolineprovidessitespecificflexibilityforinvivocollagen AT chrisjforman prolineprovidessitespecificflexibilityforinvivocollagen AT dominiquebihan prolineprovidessitespecificflexibilityforinvivocollagen AT annampuszkarska prolineprovidessitespecificflexibilityforinvivocollagen AT rakeshrajan prolineprovidessitespecificflexibilityforinvivocollagen AT davidgreid prolineprovidessitespecificflexibilityforinvivocollagen AT davidaslatter prolineprovidessitespecificflexibilityforinvivocollagen AT lucyjcolwell prolineprovidessitespecificflexibilityforinvivocollagen AT davidjwales prolineprovidessitespecificflexibilityforinvivocollagen AT richardwfarndale prolineprovidessitespecificflexibilityforinvivocollagen AT melindajduer prolineprovidessitespecificflexibilityforinvivocollagen
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Proline provides site-specific flexibility for in vivo collagen

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