Journal of Molecular Biology
Molecular packing in type I collagen fibrils
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A structural prospective for collagen receptors such as DDR and their binding of the collagen fibril
2019, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :The case of collagen's fibrillar structure or more specifically, how collagen molecules are organized within it, has been a subject of intensive study for >80 years [27–34]. Significant gains in this endeavor came with X-ray diffraction lead studies of the native, intact within the tissue, structure of type I collagen [35–51]. Following this with the formation of a coherent microfibrillar and fibrillar model based on and verified by the X-ray diffraction structure has lead to molecular visualization and molecular dynamics studies of how the collagen fibril interacts with cellular receptors [20,46,48,52–58].
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Imaging collagen type I fibrillogenesis with high spatiotemporal resolution
2015, UltramicroscopyCitation Excerpt :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]. A commonly accepted structural hierarchy of collagen starts with laterally staggered, triple-helical monomeric tropocollagen monomers (1.5 nm thick, 300 nm long), through microfibrillar units of 4–5 nm in diameter [8], to significantly larger nanometre/micrometre-sized fibrils [9].
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Collagen - Emerging collagen based therapies hit the patient
2013, Advanced Drug Delivery ReviewsCitation Excerpt :In the longitudinal direction, the molecules are supercoiled with a left handed twist. In 1987, Fraser et al. [30] assumed that the overlap zone is pseudo-hexagonal packed but the gap zone is most likely more disordered, almost liquid. According to the most recent “Microfibrillar model” proposed by Orgel et al. [31] the microfibril is formed by five one dimensionally staggered, pleated collagen molecules with a right-handed supertwist and integrated with neighbouring microfibrils.
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Visualizing molecular polar order in tissues via electromechanical coupling
2012, Journal of Structural BiologyCitation Excerpt :Collagens are present in all multicellular organisms and in many tissues, including bone, tendon, cartilage, teeth, cornea, skin, and blood vessels (Fratzl, 2008). The structure of collagen molecules and fibrils has been studied extensively by X-ray diffraction and EM techniques (Fraser et al., 1987; Hodge and Petruska, 1963; Holmes, 1996; Orgel et al., 2006; Veis et al., 1967; Wess et al., 1998). The collagen molecule consists of three hydrogen bond-stabilized polypeptide strands and has a polar orientation directed from the amine (N)-terminus toward the carboxyl (C)-terminus.