Structural mechanism studies of hTNF alpha mutants in position 30 and 42 amino acid.
- Author:
Fang HU
1
;
Shao-zhong DONG
;
Long-ding LIU
;
Shao-qing HE
;
Shu-dong ZHAO
;
Qi-han LI
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Motifs; Apoptosis; Binding Sites; Gene Expression Profiling; Humans; Molecular Structure; Mutation; Structure-Activity Relationship; Tumor Necrosis Factor-alpha; genetics; physiology
- From: Acta Academiae Medicinae Sinicae 2002;24(2):144-148
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo study the relationship between the structure and functional activity of hTNF alpha.
METHODSFour hTNF alpha mutants were constructed, different binding structures and gene responses related with these mutants were studied by the methods of immunoprecipitation and mRNA differential display.
RESULTSThe specific activities and LD50 of the different hTNF alpha mutants indicated their different bioactivities. It was shown that the hTNF alpha mutants had the relative binding affinities to the wild types. The mRNA differential display assay proved that the hTNF alpha mutants stimulated different gene responses.
CONCLUSIONThese results suggest that the specific anti-tumor activities of hTNF alpha mutants are accomplished by inducing different or same gene response at different quantities after its binding to specific receptor.
