1ILT

X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION

Summary for 1ILT

• Entry DOI: 10.2210/pdb1ilt/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: 2
• Total formula weight: 34290.81

Authors

Brandhuber, B.J.,Vigers, G.P.A. (deposition date: 1994-03-09, release date: 1995-04-01, Last modification date: 2024-02-07)

Primary citation

Vigers, G.P.,Caffes, P.,Evans, R.J.,Thompson, R.C.,Eisenberg, S.P.,Brandhuber, B.J.
X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution.
J.Biol.Chem., 269:12874-12879, 1994

PubMed Abstract: Interleukin-1 receptor antagonist (IL-1ra) is a natural competitive antagonist of IL-1. In order to further elucidate the mechanism by which IL-1ra binds without activating the IL-1 receptor, we have solved the crystal structure of IL-1ra at 2.0-A resolution. IL-1ra has the same overall beta-trefoil fold as IL-1 alpha and IL-1 beta and has a very similar hydrophobic core. However, there are a number of structural differences between the molecules, including significant differences at the open end of the beta-barrel, which has been identified in IL-1 beta as a receptor binding site.

PubMed: 8175703

Experimental method

X-RAY DIFFRACTION (2 Å)