The GTPase superfamily: conserved structure and molecular mechanism.
GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases--crystal structures, biochemical properties, or results of molecular genetic experiments--support and generate hypotheses relating structure to function in other members of the diverse family of GTPases.
Bourne
H R
HR
Department of Pharmacology, University of California, San Francisco 94143-0450.
Sanders
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DA
McCormick
F
F
D000595:Amino Acid Sequence; D000818:Animals; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000502:physiology* / Q000648:ultrastructure; D019204:GTP-Binding Proteins / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010445:Peptide Elongation Factors / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D016283:Proto-Oncogene Proteins p21(ras) / Q000378:metabolism; D015398:Signal Transduction
D010445:Peptide Elongation Factors; D010448:Peptide Initiation Factors; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D019204:GTP-Binding Proteins; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)