1ilt: Difference between revisions
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[[Image:1ilt.gif|left|200px]] | [[Image:1ilt.gif|left|200px]] | ||
'''X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1ilt |SIZE=350|CAPTION= <scene name='initialview01'>1ilt</scene>, resolution 2.0Å | |||
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'''X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ILT is a [ | 1ILT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8175703 8175703] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:57 2008'' | ||
Revision as of 09:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
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
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