Two conserved tryptophan residues of tumor necrosis factor and lymphotoxin are not involved in the biological activity
- 10 October 1988
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 238 (2) , 347-352
- https://doi.org/10.1016/0014-5793(88)80510-6
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.This publication has 14 references indexed in Scilit:
- Structure of tumour necrosis factor by X-ray solution scattering and preliminary studies by single crystal X-ray diffractionJournal of Molecular Biology, 1988
- Structure of human tumor necrosis factor .alpha. derived from recombinant DNABiochemistry, 1987
- Molecular cloning and expression of human tumor necrosis factor and comparison with mouse tumor necrosis factorEuropean Journal of Biochemistry, 1985
- Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells.The Journal of Experimental Medicine, 1985
- Is sequence conservation in interferons due to selection for functional proteins?Nature, 1985
- Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for functionNature, 1985
- Cloning and expression of cDNA for human lymphotoxin, a lymphokine with tumour necrosis activityNature, 1984
- Hemoglobin St. Claude or α2127 (H10) Lys → Thrβ2Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Two New Haemoglobin Variants involving Proline SubstitutionsNature, 1969