|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of chicken cytokine interleukin 1 beta== | | ==Crystal structure of chicken cytokine interleukin 1 beta== |
| - | <StructureSection load='2wry' size='340' side='right' caption='[[2wry]], [[Resolution|resolution]] 1.58Å' scene=''> | + | <StructureSection load='2wry' size='340' side='right'caption='[[2wry]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wry]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WRY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WRY 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=2wry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wry OCA], [http://pdbe.org/2wry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wry RCSB], [http://www.ebi.ac.uk/pdbsum/2wry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wry ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wry OCA], [https://pdbe.org/2wry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wry RCSB], [https://www.ebi.ac.uk/pdbsum/2wry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wry ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/O73909_CHICK O73909_CHICK]] Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells (By similarity).[RuleBase:RU003753] | + | [https://www.uniprot.org/uniprot/O73909_CHICK O73909_CHICK] Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells (By similarity).[RuleBase:RU003753] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 30: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Interleukin|Interleukin]] | + | *[[Interleukin 3D structures|Interleukin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Cheng, C S]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, L H]] | + | [[Category: Cheng CS]] |
| - | [[Category: Lu, W S]] | + | [[Category: Lee LH]] |
| - | [[Category: Lyu, P C]] | + | [[Category: Lu WS]] |
| - | [[Category: Wang, W C]] | + | [[Category: Lyu PC]] |
| - | [[Category: Yin, H S]] | + | [[Category: Wang WC]] |
| - | [[Category: Immune system]] | + | [[Category: Yin HS]] |
| - | [[Category: Inflammatory response]]
| + | |
| - | [[Category: Mitogen]]
| + | |
| - | [[Category: Pyrogen]]
| + | |
| Structural highlights
Function
O73909_CHICK Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells (By similarity).[RuleBase:RU003753]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cheng CS, Chen WT, Lee LH, Chen YW, Chang SY, Lyu PC, Yin HS. Structural and functional comparison of cytokine interleukin-1 beta from chicken and human. Mol Immunol. 2011 Mar;48(6-7):947-55. Epub 2011 Feb 1. PMID:21288573 doi:10.1016/j.molimm.2011.01.002
|
