Abstract
The quaternary and tertiary structure of the 20S proteasome is strictly conserved from archaea to mammals and it is assumed that its two types of subunits, termed α and β, evolved from a common ancestor protein [1–5]. In this regard the catalytically active proteasome subunits of murine 20S proteasome types display high sequence identities to each other: β1c/β1i: 63.3 %, β2c/β2i: 58.9 %, β5c/β5i: 72.4 %, β5c/β5t: 54.4 % β5i/β5t: 50.5 %.
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Huber, E.M. (2013). Results. In: Structural and Functional Characterization of the Immunoproteasome. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-01556-9_4
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DOI: https://doi.org/10.1007/978-3-319-01556-9_4
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