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- W48165669 startingPage "73" @default.
- W48165669 abstract "Elastin is the matrix protein imparting the physiologically essential properties of extensibility and elastic recoil to large arteries, lung parenchyma and other vertebrate tissues. Elastin is a polymeric protein formed from tropoelastin monomers and cross-linked, like collagens, through the side chains of lysine residues by the action of lysyl oxidase. Unlike many matrix proteins, elastin appeared relatively late in evolution, present in all species from sharks to humans, but absent at least as a vascular protein from lampreys, hagfish and other lower chordates and invertebrates. As an entropic elastomer, the polypeptide chains of elastin must remain disordered even in the polymeric state. Like many other disordered structural proteins, elastin has a low complexity, highly nonpolar and highly repetitive sequence, with the conservation of an unusual ‘style’ of sequence but an apparently relaxed requirement for precise sequence conservation, even between closely related species. Here, using both full-length and partial tropoelastin sequences representing the full range of phylogeny over which this protein is found, we describe the sequence elements and domain arrangements that are shared by all tropoelastins and are therefore likely to be required for its fundamental properties as an entropic elastomer. We then examine differences in sequence and domain arrangements between species perhaps representing adaptations to species- or tissue-specific functional requirements that may drive evolutionary changes. Finally, we consider the relationship of tropoelastins to other glycine-rich, nonpolar structural proteins that have been described in lower chordates and invertebrates and the possible evolutionary roots of this unusual protein." @default.
- W48165669 created "2016-06-24" @default.
- W48165669 creator A5016794650 @default.
- W48165669 date "2013-01-01" @default.
- W48165669 modified "2023-10-02" @default.
- W48165669 title "The Evolution of Elastin" @default.
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