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1ilt
From Proteopedia
| 1ilt, resolution 2.00Å () | |||||||||
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| Domains: | IL1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS 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.
X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution., Vigers GP, Caffes P, Evans RJ, Thompson RC, Eisenberg SP, Brandhuber BJ, J Biol Chem. 1994 Apr 29;269(17):12874-9. PMID:8175703
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ILT is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Vigers GP, Caffes P, Evans RJ, Thompson RC, Eisenberg SP, Brandhuber BJ. X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution. J Biol Chem. 1994 Apr 29;269(17):12874-9. PMID:8175703
Page seeded by OCA on Tue Feb 17 17:42:27 2009
