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| {{STRUCTURE_1md6| PDB=1md6 | SCENE= }} | | {{STRUCTURE_1md6| PDB=1md6 | SCENE= }} |
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| '''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=== |
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| ==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}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Alpha helix]] | | [[Category: Alpha helix]] |
| [[Category: Beta triple]] | | [[Category: Beta triple]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:54:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:43:06 2008'' |