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Glycine68 to Histidine73 has an important role in the function of human tumor necrosis factor alpha
Author(s) -
Cen Bo,
Jin Weixing,
Wu Haihong,
Lu Jun,
Dong Xueyin,
Xu Xianxiu
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203801
Subject(s) - alpha (finance) , mutagenesis , tumor necrosis factor alpha , mutant , escherichia coli , in vitro , function (biology) , biology , chemistry , gene , microbiology and biotechnology , biochemistry , immunology , medicine , construct validity , nursing , patient satisfaction
Mutant human tumor necrosis factor alpha(hTNF α ) genes have been constructed by in vitro mutagenesis and expressed in Escherichia coli. A deletion involving Gly68 to His73 in hTNF α remarkably decreased the solubility and biological activity of hTNF α. From the above and results of a molecular dynamics simulation it is proposed that the region of Gly68 to His73 in hTNF α has an important role in the maintenance of the 3‐D structure and modulation of the biological activity of hTNF α.