1md6
From Proteopedia
(New page: 200px<br /><applet load="1md6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1md6, resolution 1.6Å" /> '''High resolution cryst...) |
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| - | [[Image:1md6.gif|left|200px]]<br /><applet load="1md6" size=" | + | [[Image:1md6.gif|left|200px]]<br /><applet load="1md6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1md6, resolution 1.6Å" /> | caption="1md6, resolution 1.6Å" /> | ||
'''High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity'''<br /> | '''High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1MD6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1MD6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dunn, E | + | [[Category: Dunn, E F.]] |
| - | [[Category: Gay, N | + | [[Category: Gay, N J.]] |
| - | [[Category: Neill, L | + | [[Category: Neill, L A.O.]] |
| - | [[Category: Pei, X | + | [[Category: Pei, X Y.]] |
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
[[Category: beta triple]] | [[Category: beta triple]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:02 2008'' |
Revision as of 11:54, 21 February 2008
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High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity
Overview
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.
About this Structure
1MD6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity., Dunn EF, Gay NJ, Bristow AF, Gearing DP, O'Neill LA, Pei XY, Biochemistry. 2003 Sep 23;42(37):10938-44. PMID:12974628
Page seeded by OCA on Thu Feb 21 13:54:02 2008
