Crystalline three‐dimensional packing is a general characteristic of type I collagen fibrils

Jésior, Jean-Claude; Miller, A.; Berthet-Colominas, C.

doi:10.1016/0014-5793(80)80600-4

Cited by 18 publications

(7 citation statements)

References 12 publications

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“…It is well-established that collagen I fibrils form in a hierarchical self-assembly process from molecular precursors, but five decades of collagen I research have seen different models describing the precise arrangement of these molecular building blocks in mature fibrils. In particular, there has been contrasting evidence regarding the crystallinity [3,4] and/or liquid-like disorder [5,6] of structural subdomains both on the molecular and fibrillar levels, which could be related to the unique mechanical properties of collagen [7].…”

Section: Introductionmentioning

confidence: 96%

Imaging collagen type I fibrillogenesis with high spatiotemporal resolution

et al. 2015

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Section: Introductionmentioning

confidence: 96%

Imaging collagen type I fibrillogenesis with high spatiotemporal resolution

et al. 2015

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“…T h e evidence for this crystallinity is sharp Bragg reflections in the equatorial region and on the collagen helix turn layer line (at Z = (0.95 n m )-1) of the X -ray fibre p attern . M ore recent work shows th at this orderly structure occurs in m any different tissues (W ray 1971;Jesior et al 1980).…”

Section: (B) Three-dimensional Model O F Fibril (I) Evolution O F the Quasi-hexagonal Modelmentioning

confidence: 99%

Collagen: the organic matrix of bone

Miller

1984

Phil. Trans. R. Soc. Lond. B

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Collagen is the principal organic matrix in bone. The triple helical region of the molecule is 1014 amino acids long. In fibrils these molecules are staggered axially by integers of 234 residues or 68 nm (D). This axial shift occurs by self-assembly and can be understood in terms of a periodicity in the occurrence of apolar and polar residues in the amino acid sequence. Because the molecular length L = 4.47 D, there are gaps 1.5 X 36.5 nm regularly arrayed throughout the fibrils. The three-dimensional molecular arrangement is a quasi-hexagonal lattice with three distinct values for the principal interplanar spacings. Analysis of the intensity distribution in the medium-angle X-ray diffraction patterns from tendons has produced the following picture of the molecular arrangement in fibrils (Fraser et al. 1983). The molecular helices have a coherent length of 32 nm and are tilted parallel to a specific place within the lattice. A regular azimuthal interaction exists between these helices. This crystalline region could be the overlap region with a non-crystalline gap region. However, the gap is still regular axially and the molecular helices retain their structure; their lateral packing is perturbed although they retain a 'gap'. Neutron and X-ray scattering experiments have shown that calcium hydroxyapatite crystals occur in the gap and are nucleated at a specific though unknown location within the gap. The c-axis of the apatite crystals is parallel to the fibril axis and its length c = 0.688 nm is close to the axial periodicity in a protein with an extended beta-conformation. If the telopeptides at the end of a collagen molecule do have this conformation they would either have a highly heterogeneous conformation or exist in a folded manner because the overall length of the telopeptides is shorter than a regular collagen repeat of 0.029 nm would allow.

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“…The highly crystalline packing of collagen molecules in the direction of the collagen helix in some tissues in particular, allows the collection of crystalline diffraction patterns [7]. Unlike many fiber diffraction patterns which show only the unsampled molecular transform of the sample (non-crystalline diffraction arising from the helical symmetry), these patterns also contain Bragg peaks originating from the well ordered axial and lateral packing of collagen molecules into fibrils (Figure 1D).…”

Section: Introductionmentioning

confidence: 99%

Variation in the Helical Structure of Native Collagen

2014

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The structure of collagen has been a matter of curiosity, investigation, and debate for the better part of a century. There has been a particularly productive period recently, during which much progress has been made in better describing all aspects of collagen structure. However, there remain some questions regarding its helical symmetry and its persistence within the triple-helix. Previous considerations of this symmetry have sometimes confused the picture by not fully recognizing that collagen structure is a highly complex and large hierarchical entity, and this affects and is effected by the super-coiled molecules that make it. Nevertheless, the symmetry question is not trite, but of some significance as it relates to extracellular matrix organization and cellular integration. The correlation between helical structure in the context of the molecular packing arrangement determines which parts of the amino acid sequence of the collagen fibril are buried or accessible to the extracellular matrix or the cell. In this study, we concentrate primarily on the triple-helical structure of fibrillar collagens I and II, the two most predominant types. By comparing X-ray diffraction data collected from type I and type II containing tissues, we point to evidence for a range of triple-helical symmetries being extant in the molecules native environment. The possible significance of helical instability, local helix dissociation and molecular packing of the triple-helices is discussed in the context of collagen's supramolecular organization, all of which must affect the symmetry of the collagen triple-helix.

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Crystalline three‐dimensional packing is a general characteristic of type I collagen fibrils

Cited by 18 publications

References 12 publications

Imaging collagen type I fibrillogenesis with high spatiotemporal resolution

Imaging collagen type I fibrillogenesis with high spatiotemporal resolution

Collagen: the organic matrix of bone

Variation in the Helical Structure of Native Collagen

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