Structure-Expression Relationship of Tumor Necrosis Factor Receptor Mutants That Increase Expression

• Published in: The Journal of biological chemistry Vol. 278; no. 31; pp. 28961 - 28967
• Main Authors: Schweickhardt, Rene L., Jiang, Xuliang, Garone, Louise M., Brondyk, William H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2003; American Society for Biochemistry and Molecular Biology
• Subjects: Agglutinins - genetics; beta-Fructofuranosidase; Biotinylation; Cell Line; Cysteine - chemistry; Disulfides - chemistry; Gene Expression; Gene Library; Glycoside Hydrolases - genetics; Humans; Models, Molecular; Molecular Structure; Mutagenesis; Peptide Fragments - chemistry; Peptide Fragments - genetics; Peptide Fragments - metabolism; Proline; Protein Conformation; Protein Folding; Protein Structure, Quaternary; Receptors, Tumor Necrosis Factor - chemistry; Receptors, Tumor Necrosis Factor - genetics; Receptors, Tumor Necrosis Factor - metabolism; Recombinant Fusion Proteins; RNA, Messenger - analysis; Saccharomyces cerevisiae - genetics; Structure-Activity Relationship; Surface Plasmon Resonance; Thermodynamics; Transfection; Tumor Necrosis Factor-alpha - metabolism

The extracellular domain of the p55 TNF receptor (TNFrED) is an important therapeutic protein for targeting tumor necrosis factor-α (TNF-α). The expression level of the TNFrED is low for bioproduction, which is presumably associated with the complication of pairing 24 cysteine residues to form corre...