Literature DB >> 3276311

Proton NMR studies of the GDP.Mg2+ complex of the Ha-ras oncogene product p21.

I Schlichting1, A Wittinghofer, P Rösch.   

Abstract

Two-dimensional proton NMR studies were performed on the c-Ha-ras encoded proto-oncogene product p21C. COSY and NOESY spectra of the p21C.GDP.Mg2+ complex show that the ribose H1 proton of the bound GDP is in close proximity to the aromatic side chain of a phenylalanyl residue. From sequence homology with the bacterial elongation factor Tu (EF-Tu) and the known X-ray structure of the EF-Tu.GDP.Mg2+ complex it may be inferred that the Phe residue in question is either Phe78 or Phe82 in the p21 sequence.

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Year:  1988        PMID: 3276311     DOI: 10.1016/0006-291x(88)90540-2

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

1.  Structural basis of the atypical activation mechanism of KRASV14I.

Authors:  Asim K Bera; Jia Lu; Thomas E Wales; Sudershan Gondi; Deepak Gurbani; Andrew Nelson; John R Engen; Kenneth D Westover
Journal:  J Biol Chem       Date:  2019-07-24       Impact factor: 5.157

2.  Sequence-specific 1H and 15N resonance assignments and secondary structure of GDP-bound human c-Ha-Ras protein in solution.

Authors:  Y Muto; K Yamasaki; Y Ito; S Yajima; H Masaki; T Uozumi; M Wälchli; S Nishimura; T Miyazawa; S Yokoyama
Journal:  J Biomol NMR       Date:  1993-03       Impact factor: 2.835

3.  A 1H-15N NMR study of human c-Ha-ras protein: biosynthetic incorporation of 15N-labeled amino acids.

Authors:  K Yamasaki; Y Muto; Y Ito; M Wälchli; T Miyazawa; S Nishimura; S Yokoyama
Journal:  J Biomol NMR       Date:  1992-01       Impact factor: 2.835

4.  Guanine-nucleotide binding activity, interaction with GTPase-activating protein and solution conformation of the human c-Ha-Ras protein catalytic domain are retained upon deletion of C-terminal 18 amino acid residues.

Authors:  J Fujita-Yoshigaki; Y Ito; K Yamasaki; Y Muto; T Miyazawa; S Nishimura; S Yokoyama
Journal:  J Protein Chem       Date:  1992-12
  4 in total

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