View source for 8ikl


==Cryo-EM structure of the CD97-G13 complex==
<StructureSection load='8ikl' size='340' side='right'caption='[[8ikl]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ikl]] is a 4 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=8IKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IKL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.33&#8491;</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=8ikl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ikl OCA], [https://pdbe.org/8ikl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ikl RCSB], [https://www.ebi.ac.uk/pdbsum/8ikl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ikl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adhesion G protein-coupled receptors (aGPCRs) are evolutionarily ancient receptors involved in a variety of physiological and pathophysiological processes. Modulators of aGPCR, particularly antagonists, hold therapeutic promise for diseases like cancer and immune and neurological disorders. Hindered by the inactive state structural information, our understanding of antagonist development and aGPCR activation faces challenges. Here, we report the cryo-electron microscopy structures of human CD97, a prototypical aGPCR that plays crucial roles in immune system, in its inactive apo and G13-bound fully active states. Compared with other family GPCRs, CD97 adopts a compact inactive conformation with a constrained ligand pocket. Activation induces significant conformational changes for both extracellular and intracellular sides, creating larger cavities for Stachel sequence binding and G13 engagement. Integrated with functional and metadynamics analyses, our study provides significant mechanistic insights into the activation and signaling of aGPCRs, paving the way for future drug discovery efforts.

Conformational transitions and activation of the adhesion receptor CD97.,Mao C, Zhao RJ, Dong YJ, Gao M, Chen LN, Zhang C, Xiao P, Guo J, Qin J, Shen DD, Ji SY, Zang SK, Zhang H, Wang WW, Shen Q, Sun JP, Zhang Y Mol Cell. 2024 Feb 1;84(3):570-583.e7. doi: 10.1016/j.molcel.2023.12.020. Epub , 2024 Jan 11. PMID:38215752<ref>PMID:38215752</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ikl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen L]]
[[Category: Dong Y]]
[[Category: Gao M]]
[[Category: Mao C]]
[[Category: Xiao P]]
[[Category: Zhang C]]
[[Category: Zhao R]]