1ilt
From Proteopedia
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[[Image:1ilt.gif|left|200px]] | [[Image:1ilt.gif|left|200px]] | ||
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'''X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION''' | '''X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION''' | ||
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[[Category: Brandhuber, B J.]] | [[Category: Brandhuber, B J.]] | ||
[[Category: Vigers, G P.A.]] | [[Category: Vigers, G P.A.]] | ||
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Revision as of 17:08, 2 May 2008
X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION
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.
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 Fri May 2 20:08:10 2008