Structure–function analysis of human IL-1α: identification of residues required for binding to the human type I IL-1 receptor
- 1 July 1993
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 6 (5) , 535-539
- https://doi.org/10.1093/protein/6.5.535
Abstract
Using oligonucleotide-directed mutagenesis, the binding site on human interleukin-1α (IL-1α) for the human type I IL-1 receptor (IL-1R) has been analyzed. Substitution of seven amino acids (Arg12, Ile14, Asp60, Asp61, Ile64, Lys96 and Trp109) resulted in a significant loss of binding to the receptor. Based on crystallographic information, the side chains of these residues are clustered in one region of IL-1α and exposed on the surface of the protein. Five of the residues in the IL-1α binding site align with the binding residues previously determined in human IL-1β, demonstrating that the type I IL-1R recognizes homologous regions in both ligands. Unexpectedly, only three of the aligned residues are identical between IL-1α and IL-1β. These observations suggest that the composition of contact residues in the binding site is unique for each ligand–receptor complex in the IL-1 system.Keywords
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