The in situ supermolecular structure of type I collagen

J P R O Orgel; Andrew Miller; Thomas C Irving; Robert F Fischetti; Andrew P Hammersley; Tim J Wess

doi:10.1016/S0969-2126(01)00669-4

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The in situ supermolecular structure of type I collagen

Journal article

Peer reviewed

The in situ supermolecular structure of type I collagen

J P R O Orgel, Andrew Miller, Thomas C Irving, Robert F Fischetti, Andrew P Hammersley and Tim J Wess

Structure, Vol.9(11), pp.1061-1069

2001

DOI: https://doi.org/10.1016/S0969-2126(01)00669-4

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Abstract

collagen

extracellular matrix

structure

X-ray diffraction

packing

fibril

Background: The proteins belonging to the collagen family are ubiquitous throughout the animal kingdom. The most abundant collagen, type I, readily forms fibrils that convey the principal mechanical support and structural organization in the extracellular matrix of connective tissues such as bone, skin, tendon, and vasculature. An understanding of the molecular arrangement of collagen in fibrils is essential since it relates molecular interactions to the mechanical strength of fibrous tissues and may reveal the underlying molecular pathology of numerous connective tissue diseases. Results: Using synchrotron radiation, we have conducted a study of the native fibril structure at anisotropic resolution (5.4 Ã… axial and 10 Ã… lateral). The intensities of the tendon X-ray diffraction pattern that arise from the lateral packing (three-dimensional arrangement) of collagen molecules were measured by using a method analogous to Rietveld methods in powder crystallography and to the separation of closely spaced peaks in Laue diffraction patterns. These were then used to determine the packing structure of collagen by MIR. Conclusions: Our electron density map is the first obtained from a natural fiber using these techniques (more commonly applied to single crystal crystallography). It reveals the three-dimensional molecular packing arrangement of type I collagen and conclusively proves that the molecules are arranged on a quasihexagonal lattice. The molecular segments that contain the telopeptides (central to the function of collagen fibrils in health and disease) have been identified, revealing that they form a corrugated arrangement of crosslinked molecules that strengthen and stabilize the native fibril.

Details

Title: The in situ supermolecular structure of type I collagen
Authors: J P R O Orgel (Author) - University of Stirling, United Kingdom
Andrew Miller (Author) - University of Stirling, United Kingdom
Thomas C Irving (Author) - Physical Sciences Institute of Technology, United States
Robert F Fischetti (Author) - Physical Sciences Institute of Technology, United States
Andrew P Hammersley (Author) - European Synchrotron Radiation Facility, United Kingdom
Tim J Wess (Author) - European Synchrotron Radiation Facility, United Kingdom
Publication details: Structure, Vol.9(11), pp.1061-1069
Publisher: Cell Press
Date published: 2001
DOI: 10.1016/S0969-2126(01)00669-4
ISSN: 0969-2126
Organisation Unit: Office of the Deputy Vice-Chancellor (Academic); University of the Sunshine Coast, Queensland
Language: English
Record Identifier: 99451226702621
Output Type: Journal article

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Collaboration types: Domestic collaboration; International collaboration
Web Of Science research areas: Biochemistry & Molecular Biology; Biophysics; Cell Biology