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- W2985391289 abstract "s-keratin chains contain a characteristic and homologous 34-residue sequence, which is believed to adopt a twisted s-sheet conformation that assembles in an antiparallel manner with a similar sheet in a second chain to form a s-sandwich. These sandwiches are, in turn, related to one another by a left-handed four-fold screw axis to generate a helical structure that forms the core of the 3.4 nm diameter filaments observed by electron microscopy and deduced from X-ray fibre diffraction. Recently, it has been shown that one s-keratin chain, with a molecular weight approximately twice that of the majority of s-keratin chains, is conserved across the lepidosaurs (lizards, snakes and tuatara). Uniquely, it contains four 34-residue repeats. Although this chain is a minor component the observation that the entire chain shows a high degree of sequence conservation between species suggests an important structural/functional role in vivo. Modelling shows that only six families of structures are physically possible. In three of these the repeats exist within a single filament and might therefore act in a filament nucleation role. In the second three families the repeats exist in two, three or four filaments, implying that their function may be to act as an inter-filament crosslinker, thereby providing lateral reinforcement to the epidermal appendage. The favoured model is one in which the first two repeats form a β-sandwich in one filament and the second two repeats form a β-sandwich in a neighbouring filament. Links between alternating up- and down-pointing β-sheets would provide optimum connectivity." @default.
- W2985391289 created "2019-11-22" @default.
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- W2985391289 date "2020-01-01" @default.
- W2985391289 modified "2023-10-06" @default.
- W2985391289 title "Lepidosaur ß-keratin chains with four 34-residue repeats: Modelling reveals a potential filament-crosslinking role" @default.
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- W2985391289 doi "https://doi.org/10.1016/j.jsb.2019.107413" @default.
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