Glycine68 to histidine73 has an important role in the function of human tumor necrosis factor alpha

Biochem Mol Biol Int. 1997 Sep;43(1):47-52. doi: 10.1080/15216549700203801.

Abstract

Mutant human tumor necrosis factor alpha(hTNF alpha) genes have been constructed by in vitro mutagenesis and expressed in Escherichia coli. A deletion involving Gly68 to His73 in hTNF alpha remarkably decreased the solubility and biological activity of hTNF alpha. From the above and results of a molecular dynamics simulation it is proposed that the region of Gly68 to His73 in hTNF alpha has an important role in the maintenance of the 3-D structure and modulation of the biological activity of hTNF alpha.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Death
  • Cell Line
  • Computer Simulation
  • Escherichia coli / genetics
  • Humans
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / pharmacology
  • Sequence Deletion
  • Tumor Necrosis Factor-alpha / chemistry*
  • Tumor Necrosis Factor-alpha / genetics
  • Tumor Necrosis Factor-alpha / pharmacology*

Substances

  • Recombinant Proteins
  • Tumor Necrosis Factor-alpha