1ilt: Difference between revisions

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[[Image:1ilt.gif|left|200px]]
{{Seed}}
[[Image:1ilt.png|left|200px]]


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{{STRUCTURE_1ilt|  PDB=1ilt  |  SCENE=  }}  
{{STRUCTURE_1ilt|  PDB=1ilt  |  SCENE=  }}  


'''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===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_8175703}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8175703 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8175703}}


==About this Structure==
==About this Structure==
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[[Category: Vigers, G P.A.]]
[[Category: Vigers, G P.A.]]
[[Category: Cytokine]]
[[Category: Cytokine]]
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