1990
DOI: 10.1021/bi00454a026
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Proton NMR studies of transforming and nontransforming H-ras p21 mutants

Abstract: One- and two-dimensional nuclear magnetic resonance spectroscopy (1D and 2D NMR) and site-directed mutagenesis were used to study the influence of mutations on the conformation of the H-ras oncogene product p21. No severe structural differences between the different mutants, whether they were transforming or nontransforming, could be detected. Initially, selective incorporation of 3,5-deuterated tyrosyl residues into p21 and 2D NMR were used to identify the resonances representing the spin systems of the imida… Show more

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Cited by 36 publications
(32 citation statements)
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“…[15][16][17][18][19][20][21][22][23] This interaction is important for high affinity Ras nucleotide binding interactions. 34,35 The distance between the Phe 28 side-chain C 4 atom and the center of Ras-bound GDP guanine base is w3 Å . [15][16][17][18][19][20] The close n-p interaction between the side-chain of Phe 28 and the Ras-bound GDP guanine base may induce delocalization of the Phe 28 side-chain unpaired electrons to lower the redox potential of Phe 28 side-chain cation radical (Phe 28%C ) relative to the thiyl radical (i.e., Ras-S 118% ), 26-28 thereby facilitating electron transfer from the Phe 28 side-chain to Ras-S 118% .…”
Section: Resultsmentioning
confidence: 99%
“…[15][16][17][18][19][20][21][22][23] This interaction is important for high affinity Ras nucleotide binding interactions. 34,35 The distance between the Phe 28 side-chain C 4 atom and the center of Ras-bound GDP guanine base is w3 Å . [15][16][17][18][19][20] The close n-p interaction between the side-chain of Phe 28 and the Ras-bound GDP guanine base may induce delocalization of the Phe 28 side-chain unpaired electrons to lower the redox potential of Phe 28 side-chain cation radical (Phe 28%C ) relative to the thiyl radical (i.e., Ras-S 118% ), 26-28 thereby facilitating electron transfer from the Phe 28 side-chain to Ras-S 118% .…”
Section: Resultsmentioning
confidence: 99%
“…The fast cycling Ras mutation, F28L, reduces the size of the side chain at this position, which removes contacts between this residue and the guanine ring and weakens the affinity of the protein for guanine nucleotides (19). This reduced affinity allows the GTPase to spontaneously release GDP and bind GTP, even in the absence of a GEF.…”
Section: Resultsmentioning
confidence: 99%
“…These mutants have reduced affinity for nucleotides and spontaneously release GDP and bind GTP, thereby increasing levels of active GTPase within the cell (17,19). Importantly this pool of active GTPase can still hydrolyze GTP and go through the entire normal GTPase cycle (17,20).…”
mentioning
confidence: 99%
“…The conformation of the Ras protein in aqueous solution has been studied mainly by NMR spectroscopy (Schlichting et al, 1988(Schlichting et al, , 1990bCampbell-Burk, 1989;Campbell-Burk et al, 1989;Hata-Tanaka et al, 1989;Yamasaki et al, 1989;Redfield and Papastavros, 1990;Fujita-Yoshigaki et al, Miller et al, 1992;Yamasaki et al, 1992). For human N-Ras protein, selective 15N-labeling techniques have been applied for Gly and Lys residues, and selective ~3C-~SN labeling techniques (Kainosho and Tsuji, 1982) have been used for partial resonance assignments (Campbell-Burk, 1989;Campbell-Burk et al, 1989;Redfield and Papastavros, 1990).…”
Section: Introductionmentioning
confidence: 99%