Cytokine

PDB id

1irp

Contents

			Protein chain

					153 a.a. *

* Residue conservation analysis

PDB id:

1irp

Links

Name:

Cytokine

Title:

Solution structure of human interleukin-1 receptor antagonist protein

Structure:

Interleukin-1 receptor antagonist. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

12 models

Authors:

B.J.Stockman,T.A.Scahill,N.A.Strakalaitis

Key ref:

B.J.Stockman et al. (1994). Solution structure of human interleukin-1 receptor antagonist protein. FEBS Lett, 349, 79-83. PubMed id: 8045306 DOI: 10.1016/0014-5793(94)00643-1

Date:

18-Oct-94

Release date:

27-Feb-95

PROCHECK

	Headers

	References

Protein chain

P18510 (IL1RA_HUMAN) - Interleukin-1 receptor antagonist protein

Seq: Struc:					177 a.a. 153 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Gene Ontology (GO) functional annotation

Cellular component	extracellular region	4 terms
Biological process	immune response	3 terms
Biochemical function	protein binding	3 terms

DOI no: 10.1016/0014-5793(94)00643-1	FEBS Lett 349:79-83 (1994)
PubMed id: 8045306

Solution structure of human interleukin-1 receptor antagonist protein.
B.J.Stockman, T.A.Scahill, N.A.Strakalaitis, D.P.Brunner, A.W.Yem, M.R.Deibel.

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

17914732

Z.Q.Wen, X.Cao, and A.Vance (2008).
Conformation and side chains environments of recombinant human interleukin-1 receptor antagonist (rh-IL-1ra) probed by raman, raman optical activity, and UV-resonance Raman spectroscopy.

J Pharm Sci, 97, 2228-2241.

9597123

W.P.Arend, M.Malyak, C.J.Guthridge, and C.Gabay (1998).
Interleukin-1 receptor antagonist: role in biology.

Annu Rev Immunol, 16, 27-55.

7673234

S.A.Greenfeder, T.Varnell, G.Powers, K.Lombard-Gillooly, D.Shuster, K.W.McIntyre, D.E.Ryan, W.Levin, V.Madison, and G.Ju (1995).
Insertion of a structural domain of interleukin (IL)-1 beta confers agonist activity to the IL-1 receptor antagonist. Implications for IL-1 bioactivity.

J Biol Chem, 270, 22460-22466.

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