Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21.
An examination of the available amino acid sequences of GTP-binding proteins has revealed that each contains a polypeptide essentially homologous for all of them. These sequences for elongation factor-Tu (EF-Tu) and the human bladder protein p21 exhibit a singular degree of homology (50%). Chemical and structural evidence indicates that this sequence in EF-Tu constitutes part of the nucleotide-binding site. The homologous sequences may therefore contribute to the GTP-binding sites of the other proteins.
D000595:Amino Acid Sequence; D001665:Binding Sites; D006160:Guanosine Triphosphate / Q000378:metabolism; D009363:Neoplasm Proteins / Q000032:analysis* / Q000378:metabolism; D015689:Oncogene Protein p21(ras); D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000032:analysis* / Q000378:metabolism; D014404:Tubulin / Q000032:analysis / Q000378:metabolism
D009363:Neoplasm Proteins; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D014404:Tubulin; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu; D015689:Oncogene Protein p21(ras)