Characterization of ligand binding by the human p55 tumour-necrosis-factor receptor. Involvement of individual cysteine-rich repeats.

Journal article

Two soluble tumour-necrosis-factor-alpha(TNF)-binding proteins are derived from the extracellular domains of the p55 and p75 TNF receptors. They are considered to play a pivotal regulatory role in TNF-mediated inflammatory processes, including diseases such as rheumatoid arthritis, by competing with the cell surface receptors for TNF and lymphotoxin (LT, tumour-necrosis factor beta). The extracellular domains of the two receptors each contain four similar cysteine-rich repeats of about 40 ami...

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Authors: Corcoran, A; Barrett, K; Turner, M; Brown, A; Kissonerghis, A

• Publication status: Published
• Journal: European journal of biochemistry / FEBS
• Volume: 223
• Issue: 3
• Pages: 831-840
• Publication date: 1994-08-01
• DOI: 10.1111/j.1432-1033.1994.tb19059.x
• EISSN: 1432-1033
• ISSN: 0014-2956
• Language: English
• Keywords: Base Sequence; Cysteine; DNA Mutational Analysis; Antibodies, Monoclonal; Humans; Recombinant Proteins; Enzyme-Linked Immunosorbent Assay; Receptors, Tumor Necrosis Factor; Molecular Sequence Data; Cytotoxicity, Immunologic; Tumor Necrosis Factor-alpha; Antigens, CD; Ligands; Biological Assay; Receptors, Tumor Necrosis Factor, Type I; Structure-Activity Relationship; Lymphotoxin-alpha; Biosensing Techniques; Protein Conformation; Protein Binding