Differential expression and ligand binding properties of tumor necrosis factor receptor chimeric mutants.

作者: K.C. Hsu , M.V. Chao

DOI: 10.1016/S0021-9258(19)85438-8

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摘要: The receptors for tumor necrosis factor (TNF) are represented by two transmembrane proteins, p55TNFR and p75TNFR, which members of a family cell surface molecules, including the Fas antigen, CD30, CD40, OX40, Shope fibroma virus protein, low affinity p75 nerve growth receptor. A common structural feature is sequence 40 amino acids that found in adjacent repeated domains, with 6 cysteine residues conserved register. To assess functional significance this cysteine-rich domain (CRD), we have constructed chimeric between each TNF receptor cDNAs were expressed efficiently COS-1 3T3 fibroblasts, as assessed cross-linking, biotinylation immunoprecipitation, equilibrium binding. Receptors CRD either incapable binding TNF, whereas all four retained ability to bind wild type affinity. These results, conjunction previous deletion mutation studies, suggest requires repeats. Furthermore, analysis containing domains suggests cytoplasmic sequences directly influence levels expression.

参考文章(1)
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