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1ilt
From Proteopedia
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(New page: 200px<br /> <applet load="1ilt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ilt, resolution 2.0Å" /> '''X-RAY STRUCTURE OF I...)
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Revision as of 15:25, 12 November 2007
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X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147679], Mental retardation, X-linked, 21/34 OMIM:[300206]
About this Structure
1ILT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 17:31:27 2007
