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Phosphate-binding sequences in nucleotide-binding proteins.

W Möller, R Amons

    FEBS Letters
    |July 1, 1985
    PubMed
    Summary
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    Researchers identified a conserved glycine-rich motif in mononucleotide-binding proteins, crucial for phosphate binding. This sequence in oncogenic P21 proteins suggests glycine 15, not 12, is key for pyrophosphate binding.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Oncology

    Background:

    • Adenylate kinase features a conserved glycine-rich sequence (glycine XXXX glycinelysine) in its AMP/ATP phosphate-binding site.
    • This motif is present in various mononucleotide-binding proteins, including elongation factors and P21 proteins.

    Purpose of the Study:

    • To investigate the role of conserved glycine residues in pyrophosphate binding within mononucleotide-binding proteins.
    • To determine the critical glycine residue responsible for pyrophosphate binding in oncogenic P21 proteins.

    Main Methods:

    • Sequence analysis of mononucleotide-binding proteins, including P21 ras.
    • Comparison of glycine patterns in mononucleotide- vs. dinucleotide-binding proteins.
    • Structure-function prediction based on conserved amino acid residues.

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    Main Results:

    • A conserved glycine-rich motif (glycine XXXX glycinelysine) is identified in mononucleotide-binding proteins.
    • P21 ras protein exhibits a motif indicative of mononucleotide (pyro)phosphate binding.
    • A single mutation at position 12 of P21 ras can induce oncogenic activity.

    Conclusions:

    • The conserved glycine motif is critical for (pyro)phosphate binding in mononucleotide-binding proteins.
    • Glycine residue 15 in P21 ras is predicted to be more important for (pyro)phosphate binding than residue 12.
    • This finding has implications for understanding oncogenesis related to P21 ras mutations.