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Amino acid sequence restriction in relation to proteolysis.

H Jörnvall, B Persson

    Bioscience Reports
    |March 1, 1983
    PubMed
    Summary

    Proline residues often follow basic amino acids in proteins, potentially preventing unwanted cleavage. This sequence pattern, [Lys Arg]-[Lys Arg]-Pro, appears to avoid secondary structures, unlike non-proline sequences.

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    Area of Science:

    • Protein biochemistry
    • Molecular biology
    • Bioinformatics

    Background:

    • Proteolytic cleavage of pro-forms is crucial for protein maturation.
    • Specific amino acid sequences can influence protein processing and structure.
    • The role of proline in protein structure and processing is not fully understood.

    Purpose of the Study:

    • To investigate the distribution patterns of amino acid residues in proteins.
    • To explore the relationship between specific amino acid sequences and protein secondary structures.
    • To determine the potential role of proline in preventing proteolytic cleavage.

    Main Methods:

    • Analysis of amino acid residue distributions in large protein sequence databases.
    • Conformational correlation analysis to assess the adjacency of sequences to secondary structures.
    • Examination of distribution patterns in specific protein groups, such as dehydrogenases.

    Main Results:

    • Proline is overrepresented in positions following two basic residues ([Lys Arg]-[Lys Arg]).
    • [Lys Arg]-[Lys Arg]-Pro sequences are frequently not adjacent to secondary structures.
    • [Lys Arg]-[Lys Arg]-nonPro sequences are predominantly adjacent to secondary structures.

    Conclusions:

    • The [Lys Arg]-[Lys Arg]-nonPro sequence appears to be conformationally restricted in proteins.
    • Proline, alongside secondary structure elements, may serve as a mechanism to avoid undesirable proteolytic processing.
    • These findings contribute to understanding protein sequence-structure-function relationships and post-translational modifications.

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