Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation.
The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1-166) complexed to the guanosine triphosphate analogue guanosine-5'-(beta, gamma-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 A. The topological order of secondary structure elements is the same as that of the guanine-nucleotide-binding domain of bacterial elongation factor EF-Tu. Many interactions between nucleotide and protein have been identified. The effects of point mutations and the conservation of amino-acid sequence in the guanine-nucleotide-binding proteins are discussed.
Pai
E F
EF
Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, FRG.
Kabsch
W
W
Krengel
U
U
Holmes
K C
KC
John
J
J
Wittinghofer
A
A
D001665:Binding Sites; D003196:Computer Graphics; D003461:Crystallography; D000939:Epitopes; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins / Q000276:immunology / Q000648:ultrastructure*; D006165:Guanylyl Imidodiphosphate; D006801:Humans; D008274:Magnesium; D010710:Phosphates; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins / Q000276:immunology / Q000648:ultrastructure*; D016283:Proto-Oncogene Proteins p21(ras)
D000939:Epitopes; D010710:Phosphates; D011518:Proto-Oncogene Proteins; D006165:Guanylyl Imidodiphosphate; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras); D008274:Magnesium