View source for 8dso


==Structure of cIAP1, BTK and BCCov==
<StructureSection load='8dso' size='340' side='right'caption='[[8dso]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8dso]] is a 2 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=8DSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DSO 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]] 2.334&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TOO:(2~{S},4~{S})-4-[2-[2-[4-[4-[(3~{R})-3-[4-azanyl-3-(4-phenoxyphenyl)pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]-4-oxidanylidene-butyl]piperazin-1-yl]ethoxy]ethanoylamino]-1-[(2~{S})-2-cyclohexyl-2-[[(2~{S})-2-(methylamino)propanoyl]amino]ethanoyl]-~{N}-[(1~{R})-1,2,3,4-tetrahydronaphthalen-1-yl]pyrrolidine-2-carboxamide'>TOO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8dso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dso OCA], [https://pdbe.org/8dso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dso RCSB], [https://www.ebi.ac.uk/pdbsum/8dso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dso ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Targeted protein degradation using heterobifunctional chimeras holds the potential to expand target space and grow the druggable proteome. Most acutely, this provides an opportunity to target proteins that lack enzymatic activity or have otherwise proven intractable to small molecule inhibition. Limiting this potential, however, is the remaining need to develop a ligand for the target of interest. While a number of challenging proteins have been successfully targeted by covalent ligands, unless this modification affects form or function, it may lack the ability to drive a biological response. Bridging covalent ligand discovery with chimeric degrader design has emerged as a potential mechanism to advance both fields. In this work, we employ a set of biochemical and cellular tools to deconvolute the role of covalent modification in targeted protein degradation using Bruton's tyrosine kinase. Our results reveal that covalent target modification is fundamentally compatible with the protein degrader mechanism of action.

A covalent BTK ternary complex compatible with targeted protein degradation.,Schiemer J, Maxwell A, Horst R, Liu S, Uccello DP, Borzilleri K, Rajamohan N, Brown MF, Calabrese MF Nat Commun. 2023 Mar 2;14(1):1189. doi: 10.1038/s41467-023-36738-z. PMID:36864023<ref>PMID:36864023</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8dso" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Calabrese MF]]
[[Category: Schiemer JS]]