Structural Units in Collagen Fibrils

North, A. C. T.; Cowan, P.; Randall, J. T.

doi:10.1038/1741142a0

Cited by 65 publications

(14 citation statements)

References 5 publications

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“…Equatorial peaks observed on the x-ray diffraction pattern of stretched rat tail tendon fibers are evidence that specific lateral arrangements of collagen molecules occur within collagen fibrils [30]. Refinement in the quality of diffraction data allowed the definition of unit cell parameters defining possible lateral arrangement of molecules [31] that led to the proposal of a triclinic unit cell [32].…”

Section: Discussionmentioning

confidence: 97%

Viscoelastic Properties of Self-Assembled Type I Collagen Fibers: Molecular Basis of Elastic and Viscous Behaviors

Silver

Ebrahimi

Snowhill

2002

Connective Tissue Research

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We have studied the strain rate dependence of incremental stress-strain curves of self-assembled type I collagen fibers in an effort to understand the molecular phenomena that contribute to the macroscopic mechanical behavior of tendons. Results of viscoelastic tests at strain rates between 10% and 1000% per min suggest that the slope of the elastic stress-strain curve is to a first approximation independent of strain rate while the slope of the viscous stress-strain curve increases with increased strain rate. After correction of the slope of the viscous stress-strain curve for the changes in strain rate, it is observed that the apparent viscosity decreases with increased strain rate. It is concluded that the approximate strain rate independence of the elastic spring constant of collagen is consistent with the spring-like behavior of the 12 flexible regions that make up the collagen D-period. These regions are poor in the rigid amino acid residues proline and hydroxyproline. In contrast, the thixotropy of collagen is consistent with the slippage of subfibrillar subunits during tensile deformation. It is hypothesized that at high strain rates subfibrillar subunits appear to "hydroplane" by each other on a layer of loosely bound water.

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Section: Discussionmentioning

confidence: 97%

Viscoelastic Properties of Self-Assembled Type I Collagen Fibers: Molecular Basis of Elastic and Viscous Behaviors

Silver

Ebrahimi

Snowhill

2002

Connective Tissue Research

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“…The equator generally shows only a diffuse reflection at about 1.5 nm that is related to the lateral spacing of collagen molecules. Fine structure on or near the equator suggestive of lateral order was first observed by North et al (16). Additional detail has recently been obtained which offers strong support for a highly ordered substructure (1 [7][8][9][10][11][12][13][14][15][16][17][18][19].…”

Section: X-ray Diffractionmentioning

confidence: 86%

The structure of collagen fibrils

Piez

Miller

1974

J Supramol Struct

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“…A lthough the general features of the structure of type I collagen have been known for a long time, the specific packing arrangement of collagen molecules in situ has remained difficult to define, despite a great deal of effort by many investigators (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16) (the general organization of type I collagen is summarized in Fig. 5, which is published as supporting information on the PNAS web site).…”

mentioning

confidence: 99%

Microfibrillar structure of type I collagen in situ

Orgel

Irving

Miller

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

841

883

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The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three-dimensional arrangement of collagen molecules in naturally occurring fibrils. This knowledge may provide insight into key biological processes such as fibrillo-genesis and tissue remodeling and into diseases such as heart disease and cancer. Here we present a crystallographic determination of the collagen type I supermolecular structure, where the molecular conformation of each collagen segment found within the naturally occurring crystallographic unit cell has been defined (P1, a Ϸ 40.0 Å, b Ϸ 27.0 Å, c Ϸ 678 Å, ␣ Ϸ 89.2°, ␤ Ϸ 94.6°, ␥ Ϸ 105.6°; reflections: 414, overlapping, 232, and nonoverlapping, 182; resolution, 5.16 Å axial and 11.1 Å equatorial). This structure shows that the molecular packing topology of the collagen molecule is such that packing neighbors are arranged to form a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfibrils. This interdigitation establishes the crystallographic superlattice, which is formed of quasihexagonally packed collagen molecules. In addition, the molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase.x-ray ͉ fiber ͉ crystallography ͉ fibril ͉ extracellular matrix A lthough the general features of the structure of type I collagen have been known for a long time, the specific packing arrangement of collagen molecules in situ has remained difficult to define, despite a great deal of effort by many investigators (1-16) (the general organization of type I collagen is summarized in Fig. 5, which is published as supporting information on the PNAS web site). Recently, we approached this difficult structural problem by employing conventional crystallographic techniques in x-ray fiber diffraction experiments (13,17,18), culminating in an initial electron density map (13, 19) that allowed a crude look at some aspects of the supermolecular arrangement of collagen molecules in situ. Unfortunately, the high degree of disorder observed in the gap region of the electron density map precluded the fitting of a molecular model to the electron density; the gap region was largely uninterpretable. Without the structure of the gap region, it was impossible to determine the overall molecular arrangement of collagen molecules in situ, and therefore its potential for improving our understanding of the structural, developmental, and pathological function of the collagen fibril at the molecular level remained unrealized. We have subsequently integrated additional (nonoverlapping) intensity data into the structural determination process (b...

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Structural Units in Collagen Fibrils

Cited by 65 publications

References 5 publications

Viscoelastic Properties of Self-Assembled Type I Collagen Fibers: Molecular Basis of Elastic and Viscous Behaviors

Viscoelastic Properties of Self-Assembled Type I Collagen Fibers: Molecular Basis of Elastic and Viscous Behaviors

The structure of collagen fibrils

Microfibrillar structure of type I collagen in situ

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