1md6: Difference between revisions

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[[Image:1md6.gif|left|200px]]
[[Image:1md6.gif|left|200px]]


{{Structure
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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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[[Category: Neill, L A.O.]]
[[Category: Neill, L A.O.]]
[[Category: Pei, X Y.]]
[[Category: Pei, X Y.]]
[[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 Sun Mar 30 22:14:37 2008''

Revision as of 21:54, 2 May 2008

File:1md6.gif

Template:STRUCTURE 1md6

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 Sat May 3 00:54:12 2008

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