Abstract
Domains of aspartic proteinase molecules have the same fold (Tang et al., 1978) while their primary structures show no homology except small segments of a few amino acid residues located in the region of the active site in the three-dimensional structure. One may ask: is it possible to detect a common specific property of amino acid sequences of both domains which can explain the tendency of their chains to fold by the same manner? In other words does a consensus template for the specific aspartic proteinase fold exist? Interactions between different segments of a polypeptide chain providing formation of a central hydrophobic core of a protein molecule determine mainly the geometrical type of protein folding. If a consensus template for the specific aspartic proteinase fold really exists it must concern the formation of central hydrophobic cores in domains.
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© 1991 Plenum Press, New York
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Andreeva, N.S. (1991). A Consensus Template for the Aspartic Proteinase Fold. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_77
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_77
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