Title : Structural changes induced in p21Ras upon GAP-334 complexation as probed by ESEEM spectroscopy and molecular-dynamics simulation.

Pub. Date : 2000 Dec 15

PMID : 11188692






6 Functional Relationships(s)
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Protein Name
Organism
1 This change significantly reduces the distances from the amide groups of p21 glycine residues 60 and 13 to the divalent metal ion. Glycine H3 histone pseudogene 16 Homo sapiens
2 CONCLUSIONS: The movement of glycine residues 60 and 13 upon the binding of GAP-334 in solution provides a physical basis to interpret prior mutagenesis studies, which indicated that Gly-60 and Gly-13 of p21 play important roles in the GAP-dependent GTPase reaction. Glycine H3 histone pseudogene 16 Homo sapiens
3 CONCLUSIONS: The movement of glycine residues 60 and 13 upon the binding of GAP-334 in solution provides a physical basis to interpret prior mutagenesis studies, which indicated that Gly-60 and Gly-13 of p21 play important roles in the GAP-dependent GTPase reaction. Glycine H3 histone pseudogene 16 Homo sapiens
4 CONCLUSIONS: The movement of glycine residues 60 and 13 upon the binding of GAP-334 in solution provides a physical basis to interpret prior mutagenesis studies, which indicated that Gly-60 and Gly-13 of p21 play important roles in the GAP-dependent GTPase reaction. Glycine H3 histone pseudogene 16 Homo sapiens
5 Gly-60 and Gly-13 may play direct catalytic roles and stabilize the attacking water molecule and beta,gamma-bridging oxygen, respectively, in p21. Glycine H3 histone pseudogene 16 Homo sapiens
6 Gly-60 and Gly-13 may play direct catalytic roles and stabilize the attacking water molecule and beta,gamma-bridging oxygen, respectively, in p21. Glycine H3 histone pseudogene 16 Homo sapiens