View source for 9ogw


==Identification of ligands for E3 ligases using fragment-based methods==
<StructureSection load='9ogw' size='340' side='right'caption='[[9ogw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ogw]] 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=9OGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OGW 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1CA8:2-{[(thiophen-3-yl)methyl]amino}benzoic+acid'>A1CA8</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=9ogw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ogw OCA], [https://pdbe.org/9ogw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ogw RCSB], [https://www.ebi.ac.uk/pdbsum/9ogw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ogw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBLC_HUMAN CBLC_HUMAN] Regulator of EGFR mediated signal transduction.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heterobifunctional molecules that induce targeted degradation have emerged as powerful tools in chemical biology, target validation, and drug discovery. Despite their promise, the field is constrained by the relative paucity of ligands available for E3 ligases. Expanding the ligand repertoire for E3 ligases and other components of ubiquitin-proteasome system could significantly broaden the scope of the targeted degradation field. In this study, we report the identification of ligands for non-essential E3 ligases that are preferentially expressed in cancer tissues relative to normal tissues. Using a protein-observed NMR-based fragment screen, an ideal technique for this purpose, we identified fragment ligands and characterized their binding modes by X-ray crystallography. These ligands represent promising starting points for further optimization toward the discovery of tumor-selective degraders that may enhance the therapeutic window targeting proteins for which inhibition or degradation is associated with systemic toxicity.

Identification of ligands for E3 ligases with restricted expression using fragment-based methods.,Waterson AG, Lehmann BD, Lu Z, Sensintaffar JL, Olejniczak ET, Zhao B, Rietz T, Payne WG, Phan J, Fesik SW RSC Chem Biol. 2025 Oct 2. doi: 10.1039/d5cb00198f. PMID:41070186<ref>PMID:41070186</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ogw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fesik SW]]
[[Category: Phan J]]