Abstract
The structural evidence suggests that the eukaryotic aspartic proteases and the retroviral proteases are related in three-dimensional structures and in their evolution. The internal two-fold structural homology between the two lobes of the eukaryotic aspartic proteases (Tang et al., 1978) is similar to the homodimeric structure of HIV (Wlodawer et al., 1989) and other retroviral proteases. Also, the folding topology of individual lobes in eukaryotic aspartic proteases is related to that of the retroviral enzyme monomers (Rao et al., 1991). It is now well established that these two groups of proteases share active-site structure and catalytic mechanism.
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Koelsch, G., Loy, J., Lin, X., Tang, J. (1998). Activation Mechanism of Pepsinogen as Compared to the Processing of HIV Protease gag-pol Precursor Protein. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_34
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DOI: https://doi.org/10.1007/978-1-4615-5373-1_34
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