PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9778364-6 1998 Near- and far-UV circular dichroism spectra of these three forms of p21(H-ras) show that removal of the Mg2+ from the ternary complex loosens the aromatic side chain packing but leaves the secondary structure largely unchanged. magnesium ion 104-108 H3 histone pseudogene 16 Homo sapiens 68-71 9778364-8 1998 These results demonstrate that ligands play a significant role in the stability and structure of the p21.GDP.Mg2+ complex. magnesium ion 109-113 H3 histone pseudogene 16 Homo sapiens 101-104 9778365-1 1998 p21(H-ras) plays a critical role in signal transduction pathways by cycling between an active, GTP/Mg2+ ternary complex and an inactive, GDP/Mg2+ complex. magnesium ion 99-103 H3 histone pseudogene 16 Homo sapiens 0-3 9778365-1 1998 p21(H-ras) plays a critical role in signal transduction pathways by cycling between an active, GTP/Mg2+ ternary complex and an inactive, GDP/Mg2+ complex. magnesium ion 141-145 H3 histone pseudogene 16 Homo sapiens 0-3 9778365-11 1998 Only the faster unfolding reaction is observed in the absence of Mg2+, suggesting that this reaction corresponds to the unfolding of the binary complex, p21(H-ras)*GDP. magnesium ion 65-69 H3 histone pseudogene 16 Homo sapiens 153-156 9778365-14 1998 The kinetic data show that the refolding/unfolding of p21(H-ras) occurs through parallel channels that are strongly influenced by the binding/release of GDP and Mg2+ to/from a pair of native conformers. magnesium ion 161-165 H3 histone pseudogene 16 Homo sapiens 54-57 26148683-2 2015 The progressive substitution of the paramagnetic Co(2+) high spin ion by the diamagnetic Mg(2+), of about the same size, induces changes in the room temperature crystal structure, from a distorted P2(1)/n phase for the undoped Sr(2)CoTeO(6) oxide to the I4/m of the end member (Sr(2)MgTeO(6)). magnesium ion 89-95 H3 histone pseudogene 16 Homo sapiens 197-202 9309221-3 1997 The coordination of the p21 residue Thr35 to Mg2+ in its active site, which has been observed in the crystal structure of p21 in complex with a GTP-analog GMPPNP but not with GDP, has been proposed to drive the conformational change accompanying nucleotide substitution and may have a role in the GTP hydrolysis reaction itself. magnesium ion 45-49 H3 histone pseudogene 16 Homo sapiens 24-27 9309221-3 1997 The coordination of the p21 residue Thr35 to Mg2+ in its active site, which has been observed in the crystal structure of p21 in complex with a GTP-analog GMPPNP but not with GDP, has been proposed to drive the conformational change accompanying nucleotide substitution and may have a role in the GTP hydrolysis reaction itself. magnesium ion 45-49 H3 histone pseudogene 16 Homo sapiens 122-125 9112760-2 1997 Picomolar Al3+ concentrations inhibited the GTPase activity of ras p21 in an Mg(2+)-dependent manner, consistent with an Al3+/Mg2+ competition mechanism. magnesium ion 77-83 H3 histone pseudogene 16 Homo sapiens 67-70 9112760-2 1997 Picomolar Al3+ concentrations inhibited the GTPase activity of ras p21 in an Mg(2+)-dependent manner, consistent with an Al3+/Mg2+ competition mechanism. magnesium ion 126-130 H3 histone pseudogene 16 Homo sapiens 67-70 9112760-5 1997 Further dissection of the ras p21 cycle revealed that Mg(2+)-dependent GDP/GTP exchange was the Al(3+)-sensitive step. magnesium ion 54-60 H3 histone pseudogene 16 Homo sapiens 30-33 8419371-1 1993 The coordination and binding of the Mg2+ ion in the nucleotide-binding site of p21 have been investigated using site-directed mutagenesis, kinetic methods, and phosphorous NMR. magnesium ion 36-40 H3 histone pseudogene 16 Homo sapiens 79-82 8419371-2 1993 Mg2+ in the p21.nucleotide.Mg2+ complex appears to be in fast equilibrium with the solvent. magnesium ion 0-4 H3 histone pseudogene 16 Homo sapiens 12-15 8419371-2 1993 Mg2+ in the p21.nucleotide.Mg2+ complex appears to be in fast equilibrium with the solvent. magnesium ion 27-31 H3 histone pseudogene 16 Homo sapiens 12-15 8419371-3 1993 The dissociation constant between Mg2+ and the p21.GDP complex was determined to be 2.8 microM. magnesium ion 34-38 H3 histone pseudogene 16 Homo sapiens 47-50 1740128-6 1992 The concentrations of Mg2+ influencing the dissociation rate of the p21.GDP complex are much higher than for the intrinsic GTPase activity, an effect also observed for EF-Tu. magnesium ion 22-26 H3 histone pseudogene 16 Homo sapiens 68-71 2405906-7 1990 In solution, the p21-bound GDP.Mg2+ has an anti conformation, and the phenyl ring of Phe28 is close to the ribose of the bound GDP.Mg2+. magnesium ion 31-35 H3 histone pseudogene 16 Homo sapiens 17-20 2405906-7 1990 In solution, the p21-bound GDP.Mg2+ has an anti conformation, and the phenyl ring of Phe28 is close to the ribose of the bound GDP.Mg2+. magnesium ion 131-135 H3 histone pseudogene 16 Homo sapiens 17-20 3276311-0 1988 Proton NMR studies of the GDP.Mg2+ complex of the Ha-ras oncogene product p21. magnesium ion 30-34 H3 histone pseudogene 16 Homo sapiens 74-77 3276311-3 1988 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. magnesium ion 118-122 H3 histone pseudogene 16 Homo sapiens 215-218 3298232-5 1987 The association rate constant for p21 and GDP is 1.47 X 10(6) M-1 s-1 and for GTP is 2.9 X 10(6) M-1 s-1 at 0 degree C. By using appropriately determined dissociation rate constants we have determined the binding constant for p21.GDP and p21.GTP in the presence of excess Mg2+ to be 5.7 X 10(10) M-1 and 6.0 X 10(10) M-1, respectively, at 0 degree C. magnesium ion 272-276 H3 histone pseudogene 16 Homo sapiens 34-37 3298232-5 1987 The association rate constant for p21 and GDP is 1.47 X 10(6) M-1 s-1 and for GTP is 2.9 X 10(6) M-1 s-1 at 0 degree C. By using appropriately determined dissociation rate constants we have determined the binding constant for p21.GDP and p21.GTP in the presence of excess Mg2+ to be 5.7 X 10(10) M-1 and 6.0 X 10(10) M-1, respectively, at 0 degree C. magnesium ion 272-276 H3 histone pseudogene 16 Homo sapiens 226-229 3298232-5 1987 The association rate constant for p21 and GDP is 1.47 X 10(6) M-1 s-1 and for GTP is 2.9 X 10(6) M-1 s-1 at 0 degree C. By using appropriately determined dissociation rate constants we have determined the binding constant for p21.GDP and p21.GTP in the presence of excess Mg2+ to be 5.7 X 10(10) M-1 and 6.0 X 10(10) M-1, respectively, at 0 degree C. magnesium ion 272-276 H3 histone pseudogene 16 Homo sapiens 226-229 8223583-13 1993 Monomeric rac1 p21 exhibited an almost absolute dependence on exogenous GTP following removal of the endogenous nucleotide in low Mg2+ solution. magnesium ion 130-134 H3 histone pseudogene 16 Homo sapiens 15-18