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1ilt

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[[Image:1ilt.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1ilt| PDB=1ilt | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ilt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilt OCA], [http://www.ebi.ac.uk/pdbsum/1ilt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ilt RCSB]</span>
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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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[[Category: cytokine]]
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[[Category: Cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:08:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:28 2008''
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Revision as of 17:08, 2 May 2008

Image:1ilt.gif

Template:STRUCTURE 1ilt

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

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