Glycine68 to histidine73 has an important role in the function of human tumor necrosis factor alpha.
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.
Cen
B
B
State Key Laboratory of Pharmaceutical Biotechnology, Department of Biochemistry, Nanjing University, People's Republic of China.
Jin
W
W
Wu
H
H
Lu
J
J
Dong
X
X
Xu
X
X
D000595:Amino Acid Sequence; D000818:Animals; D016923:Cell Death; D002460:Cell Line; D003198:Computer Simulation; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000494:pharmacology; D017384:Sequence Deletion; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*
D011994:Recombinant Proteins; D014409:Tumor Necrosis Factor-alpha