title: Two conserved tryptophan residues of tumor necrosis factor and lymphotoxin are not involved in the biological activity.
abstract: Each of the two highly conserved tryptophan residues in hTNF (positions 28 and 114) was converted into phenylalanine by site-directed mutagenesis and the mutant proteins were partially purified. A cytotoxicity assay on mouse L929 cells showed only a slight reduction in biological activity, strongly suggesting that neither of the two amino acids is involved in the active site.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002470:Cell Survival; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004274:DNA, Recombinant; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D008233:Lymphotoxin-alpha / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation; D010649:Phenylalanine; D010957:Plasmids; D013329:Structure-Activity Relationship; D014170:Transformation, Genetic; D014364:Tryptophan; D014409:Tumor Necrosis Factor-alpha / Q000235:genetics / Q000502:physiology*
chemical_list: D004274:DNA, Recombinant; D008233:Lymphotoxin-alpha; D014409:Tumor Necrosis Factor-alpha; D010649:Phenylalanine; D014364:Tryptophan; D004247:DNA