3nj5: Difference between revisions

<StructureSection load='3nj5' size='340' side='right' caption='[[3nj5]], [[Resolution|resolution]] 1.67&Aring;' scene=''>

<table><tr><td colspan='2'>[[3nj5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NJ5 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nj5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nj5 RCSB], [http://www.ebi.ac.uk/pdbsum/3nj5 PDBsum]</span></td></tr>

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== Publication Abstract from PubMed ==

Interleukin-1 beta (IL-1beta) is an important cytokine in the immune system. The properties of avian IL-1betas are less well understood than the mammalian IL-1betas, and there is no available structure of avian IL-1betas in the Protein Data Bank. Here, we report the crystal structures of wild-type and Y157F mutant IL-1betas from chicken. Both the wild-type and mutant IL-1betas share a beta-trefoil conformation similar to that of human IL-1beta and also have an internal hydrophobic cavity. However, the cavity sizes clearly differ from that of human IL-1beta due to the packing of hydrophobic residues. Our studies also reveal that the relative thermal stability of IL-1betas does not correlate with cavity size but rather is dependent on the amino acid residues present around the cavity. This cavity serves as a scaffold for maintaining the structure of the IL-1beta core region but does not have a biological function per se. Moreover, we found that human IL-1beta cannot induce chemokine expression in chicken fibroblasts or elevate plasma cortisol levels in chickens, implying a lack of cross-species bioactivity. Close examination reveals that significant structural and sequence differences occur in the terminal and some loop regions between human and chicken IL-1betas. These variable regions have been shown to be critical for receptor binding, thus resulting in a lack of species cross-reactivity between human and chicken IL-1beta.

 

Structural and functional comparison of cytokine interleukin-1 beta from chicken and human.,Cheng CS, Chen WT, Lee LH, Chen YW, Chang SY, Lyu PC, Yin HS Mol Immunol. 2011 Mar;48(6-7):947-55. Epub 2011 Feb 1. PMID:21288573<ref>PMID:21288573</ref>

 

*[[Interleukin|Interleukin]]

[[Category: Chen, Y W]]

[[Category: Yin, H S]]

[[Category: Chicken]]

[[Category: Interleukin-1 beta]]