2mib
From Proteopedia
(Difference between revisions)
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<StructureSection load='2mib' size='340' side='right'caption='[[2mib]], [[Resolution|resolution]] 2.84Å' scene=''> | <StructureSection load='2mib' size='340' side='right'caption='[[2mib]], [[Resolution|resolution]] 2.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2mib]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2mib]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MIB FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84Å</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=2mib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mib OCA], [https://pdbe.org/2mib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mib RCSB], [https://www.ebi.ac.uk/pdbsum/2mib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mib ProSAT]</span></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=2mib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mib OCA], [https://pdbe.org/2mib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mib RCSB], [https://www.ebi.ac.uk/pdbsum/2mib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mib ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/IL1B_MOUSE IL1B_MOUSE] 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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2mib ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2mib ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The three-dimensional structure of recombinant murine interleukin-1 beta has been solved by X-ray crystallographic techniques to 2.8 A resolution and refined to a crystallographic R factor of 0.192. Although murine interleukin-1 beta crystallizes in the same space group as human interleukin-1 beta with almost identical unit cell dimensions, the packing of the molecules is quite different. The murine interleukin-1 beta structure was solved by molecular replacement using the refined structure of human interleukin-1 beta as trial structure, and found to be related to the human structure by a nearly perfect twofold rotation about the crystallographic y-axis and a 14 degrees rotation about the z-axis, with no translation. The folding of murine interleukin-1 beta is similar to that found for the human variant, consisting of 12 beta strands wrapped around a core of hydrophobic side chains in a tetrahedron-like fashion. Significant differences with respect to the human structure are seen at the N terminus and in 4 of the 11 loops connecting the 12 beta strands. | ||
- | |||
- | The structure of murine interleukin-1 beta at 2.8 A resolution.,van Oostrum J, Priestle JP, Grutter MG, Schmitz A J Struct Biol. 1991 Oct;107(2):189-95. PMID:1807351<ref>PMID:1807351</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2mib" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Interleukin 3D structures|Interleukin 3D structures]] | *[[Interleukin 3D structures|Interleukin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Gruetter | + | [[Category: Gruetter MG]] |
- | + | [[Category: Priestle JP]] | |
- | [[Category: Priestle | + | [[Category: Schmitz A]] |
- | [[Category: Schmitz | + | [[Category: Van Oostrum J]] |
- | [[Category: | + |
Current revision
THE STRUCTURE OF MURINE INTERLEUKIN-1 BETA AT 2.8 ANGSTROMS RESOLUTION
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