1IRP

SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN

Summary for 1IRP

• Entry DOI: 10.2210/pdb1irp/pdb
• Descriptor: INTERLEUKIN-1 RECEPTOR ANTAGONIST (1 entity in total)
• Functional Keywords: cytokine
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Secreted. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: P18510
• Total number of polymer chains: 1
• Total formula weight: 17276.60

Authors

Stockman, B.J.,Scahill, T.A.,Strakalaitis, N.A. (deposition date: 1994-10-18, release date: 1995-02-27, Last modification date: 2024-05-22)

Primary citation

Stockman, B.J.,Scahill, T.A.,Strakalaitis, N.A.,Brunner, D.P.,Yem, A.W.,Deibel Jr., M.R.
Solution structure of human interleukin-1 receptor antagonist protein.
FEBS Lett., 349:79-83, 1994

PubMed Abstract: 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.

PubMed: 8045306
DOI: 10.1016/0014-5793(94)00643-1

Experimental method

SOLUTION NMR