期刊论文详细信息
FEBS Letters
Phosphate‐binding sequences in nucleotide‐binding proteins
Möller, W.1  Amons, R.1 
[1] Department of Medical Biochemistry, Sylvius Laboratories, PO Box 9503, 2300 RA Leiden, The Netherlands
关键词: Mononucleotide-binding protein;    Dinucleotide-binding protein;    Adenylate kinase;    Elongation factor P21;    Ras protein;    Phosphate-binding region;   
DOI  :  10.1016/0014-5793(85)81326-0
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

In the three-dimensional model of adenylate kinase, the phosphate-binding site for AMP and ATP has been identified [Pai, E.F. et al. (1977) J. Mol. Biol. 114, 37-45]. In this region one can distinguish a sequence glycine XXXX glycinelysine. The same sequence is found in many other mononucleotide-binding proteins including elongation factors and oncogenic P21 proteins. Dinucleotide-binding proteins display a pyrophosphate-binding unit with a glycine pattern different from that of mononucleotide-binding proteins. It has been found that P21 ras protein possesses a strand motif typical for (pyro)phosphate binding of a mononucleotide. A single mutation at position 12 can confer oncogenic activity on the protein. Based on the assumption that amino acid residues which are critical for function are preferentially conserved, we predict from the sequence that glycine residue 15 rather than residue 12 is important for (pyro)phosphate binding.

【 授权许可】

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