Solution structure of human interleukin-1 receptor antagonist protein.
Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. In contrast to IL-1 beta, 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-1 beta. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins.
Stockman
B J
BJ
Upjohn Laboratories, Upjohn Company, Kalamazoo, MI 49007.
Scahill
T A
TA
Strakalaitis
N A
NA
Brunner
D P
DP
Yem
A W
AW
Deibel
M R
MR
D000595:Amino Acid Sequence; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1 / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017472:Receptors, Interleukin-1 / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D012795:Sialoglycoproteins / Q000737:chemistry*; D012996:Solutions
C507763:IL1RN protein, human; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1; D017472:Receptors, Interleukin-1; D011994:Recombinant Proteins; D012795:Sialoglycoproteins; D012996:Solutions