A Consensus Template for the Aspartic Proteinase Fold
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.
KeywordsHydrophobic Residue Aspartic Proteinase Align Amino Acid Sequence Template Region Bovine Chymosin
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- Andreeva, N., 1988, “Structure and Biosynthesis of Proteins (Puschino),” 3: 97–115.Google Scholar
- Foltmann, B., 1988, in: “Abstracts of 18th Linderstrøm-Lang Conference” pp.7–20.Google Scholar
- Pechik, I. V., Gustchina, A. E., Andreeva, N. S. & Fedorov, A. A., 1988, “Structure and Biosynthesis of Proteins (Pustchino),” 3: 87–96.Google Scholar