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Solution structure of human interleukin‐1 receptor antagonist protein
Author(s) -
Stockman Brian J.,
Scahill Terrence A.,
Strakalaitis Nancy A.,
Brunner David P.,
Yem Anthony W.,
Deibel Martin R.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00643-1
Subject(s) - receptor , interleukin 1 receptor antagonist , residue (chemistry) , interleukin 1 receptor , chemistry , homologous chromosome , 5 ht5a receptor , amino acid residue , peptide sequence , enzyme linked receptor , protein structure , biochemistry , protein superfamily , biology , receptor antagonist , antagonist , microbiology and biotechnology , interleukin , genetics , gene , cytokine
Interleukin‐1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin‐1 receptor. In contrast to IL‐1β IRAP binds to the IL‐1 receptor but does not elicit a physiological response. We have determined the solution structure of IRAP using NMR spectroscopy. While the overall topology of the two 153‐residue proteins is quite similar, functionally critical differences exist concerning the residues of the linear amino acid sequence that constitute structurally homologous regions in the two proteins. Structurally homologous residues important for IL‐1 receptor binding are conserved between IRAP and IL‐1β. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins.