X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution.
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.
Vigers
G P
GP
Synergen, Inc., Boulder, Colorado 80301.
Caffes
P
P
Evans
R J
RJ
Thompson
R C
RC
Eisenberg
S P
SP
Brandhuber
B J
BJ
D000595:Amino Acid Sequence; D003196:Computer Graphics; D006801:Humans; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1 / Q000737:chemistry; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D012795:Sialoglycoproteins / Q000737:chemistry*; D014961:X-Ray Diffraction
C507763:IL1RN protein, human; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1; D012795:Sialoglycoproteins