Abstract
The first crystal structures of members of the aspartic proteinase family were discussed at the 1976 Conference in Norman, Oklahoma [1]. Since that time, an increasingly rapid stream of structural information has issued from the crystallography groups [2]. At this point it is clear that members of this family are closely related structurally, with a central core composed of two domains, each of which has a two-layered β-sheet arrangement (see Figure 1 for an overall representation of a typical aspartic proteinase).
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Dunn, B.M., Scarborough, P.E., Lowther, W.T., Rao-Naik, C. (1995). Comparison of the Active Site Specificity of the Aspartic Proteinases Based on a Systematic Series of Peptide Substrates. In: Takahashi, K. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 362. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1871-6_1
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DOI: https://doi.org/10.1007/978-1-4615-1871-6_1
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