Title : The frozen solution structure of p21 ras determined by ESEEM spectroscopy reveals weak coordination of Thr35 to the active site metal ion.

Pub. Date : 1997 Aug 15

PMID : 9309221






5 Functional Relationships(s)
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1 Hydrolysis of tightly bound GTP alters the conformation of p21, terminating the signal. Guanosine Triphosphate H3 histone pseudogene 16 Homo sapiens
2 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. Guanosine Triphosphate H3 histone pseudogene 16 Homo sapiens
3 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. Guanosine Triphosphate H3 histone pseudogene 16 Homo sapiens
4 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. Guanosine Triphosphate H3 histone pseudogene 16 Homo sapiens
5 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. Guanosine Triphosphate H3 histone pseudogene 16 Homo sapiens