View source for 7ydp


==Cryo-EM structure of CD97/miniGs complex==
<StructureSection load='7ydp' size='340' side='right'caption='[[7ydp]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ydp]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YDP 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]] 3.1&#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=7ydp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ydp OCA], [https://pdbe.org/7ydp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ydp RCSB], [https://www.ebi.ac.uk/pdbsum/7ydp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ydp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CD97 (ADGRE5) is an adhesion G protein-coupled receptor (aGPCR) which plays crucial roles in immune system and cancer. However, the mechanism of CD97 activation and the determinant of G(13) coupling selectivity remain unknown. Here, we present the cryo-electron microscopy structures of human CD97 in complex with G(13), G(q), and G(s). Our structures reveal the stalk peptide recognition mode of CD97, adding missing information of the current tethered-peptide activation model of aGPCRs. For instance, a revised "FXphiphiphi" motif and a framework of conserved aromatic residues in the ligand-binding pocket. Importantly, structural comparisons of G(13), G(q), and G(s) engagements of CD97 reveal key determinants of G(13) coupling selectivity, where a deep insertion of the alpha helix 5 and a closer contact with the transmembrane helix 6, 5, and 3 dictate coupling preferences. Taken together, our structural study of CD97 provides a framework for understanding CD97 signaling and the G(13) coupling selectivity.

Structural basis of CD97 activation and G-protein coupling.,Wang N, Qian Y, Xia R, Zhu X, Xiong Y, Zhang A, Guo C, He Y Cell Chem Biol. 2023 Nov 16;30(11):1343-1353.e5. doi: , 10.1016/j.chembiol.2023.08.003. Epub 2023 Sep 5. PMID:37673067<ref>PMID:37673067</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ydp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: He Y]]
[[Category: Wang N]]