1md6: Difference between revisions

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[[Image:1md6.gif|left|200px]]
{{Seed}}
[[Image:1md6.png|left|200px]]


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{{STRUCTURE_1md6|  PDB=1md6  |  SCENE=  }}  
{{STRUCTURE_1md6|  PDB=1md6  |  SCENE=  }}  


'''High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity'''
===High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity===




==Overview==
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Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 family are involved in innate immune responses to infection and injury. These cytokines bind to specific receptors and cause activation of NFkappaB and MAP kinase. IL-1F5 has a sequence identity of 44% to IL-1 receptor antagonist (IL-1Ra), a natural antagonist of the IL-1 system. Here we report the crystal structure of IL-1F5 to a resolution of 1.6 A. It has the same beta-trefoil fold as other IL-1 family members, and the hydrophobic core is well conserved. However, there are substantial differences in the loop conformations, structures that confer binding specificity for the cognate receptor to IL-1beta and the antagonist IL-1Ra. Docking and superimposition of the IL-1F5 structure suggest that is unlikely to bind to the interleukin1 receptor, consistent with biochemical studies. The structure IL-1F5 lacks features that confer antagonist properties on IL-1Ra, and we predict that like IL-1beta it will act as an agonist. These studies give insights into how distinct receptor specificities can evolve within related cytokine families.
The line below this paragraph, {{ABSTRACT_PUBMED_12974628}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12974628 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12974628}}


==About this Structure==
==About this Structure==
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[[Category: Alpha helix]]
[[Category: Alpha helix]]
[[Category: Beta triple]]
[[Category: Beta triple]]
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