View source for 8rys


==Human IL-1beta, unliganded==
<StructureSection load='8rys' size='340' side='right'caption='[[8rys]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rys]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RYS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=8rys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rys OCA], [https://pdbe.org/8rys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rys RCSB], [https://www.ebi.ac.uk/pdbsum/8rys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rys ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IL1B_HUMAN IL1B_HUMAN] 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.<ref>PMID:3920526</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human interleukin-1beta (IL-1beta) is a pro-inflammatory cytokine that plays a critical role in the regulation of the immune response and the development of various inflammatory diseases. In this publication, we disclose our efforts toward the discovery of IL-1beta binders that interfere with IL-1beta signaling. To this end, several technologies were used in parallel, including fragment-based screening (FBS), DNA-encoded library (DEL) technology, peptide discovery platform (PDP), and virtual screening. The utilization of distinct technologies resulted in the identification of new chemical entities exploiting three different sites on IL-1beta, all of them also inhibiting the interaction with the IL-1R1 receptor. Moreover, we identified lysine 103 of IL-1beta as a target residue suitable for the development of covalent, low-molecular-weight IL-1beta antagonists.

Ligandability Assessment of IL-1beta by Integrated Hit Identification Approaches.,Vulpetti A, Rondeau JM, Bellance MH, Blank J, Boesch R, Boettcher A, Bornancin F, Buhr S, Connor LE, Dumelin CE, Esser O, Hediger M, Hintermann S, Hommel U, Koch E, Lapointe G, Leder L, Lehmann S, Lehr P, Meier P, Muller L, Ostermeier D, Ramage P, Schiebel-Haddad S, Smith AB, Stojanovic A, Velcicky J, Yamamoto R, Hurth K J Med Chem. 2024 May 10. doi: 10.1021/acs.jmedchem.4c00240. PMID:38728572<ref>PMID:38728572</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rys" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Lehmann S]]
[[Category: Rondeau J-M]]