View source for 9dak


==Merbecovirus PnNL2018B Spike glycoprotein RBD bound to the P. Nathusii ACE2==
<StructureSection load='9dak' size='340' side='right'caption='[[9dak]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9dak]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Merbecovirus Merbecovirus] and [https://en.wikipedia.org/wiki/Pipistrellus_nathusii Pipistrellus nathusii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DAK 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=9dak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dak OCA], [https://pdbe.org/9dak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dak RCSB], [https://www.ebi.ac.uk/pdbsum/9dak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dak ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The angiotensin-converting enzyme 2 (ACE2) receptor is shared by various coronaviruses with distinct receptor-binding domain (RBD) architectures, yet our understanding of these convergent acquisition events remains elusive. Here, we report that two bat MERS-related coronaviruses (MERSr-CoVs) infecting Pipistrellus nathusii (P.nat)-MOW15-22 and PnNL2018B-use ACE2 as their receptor, with narrow ortholog specificity. Cryoelectron microscopy structures of the MOW15-22/PnNL2018B RBD-ACE2 complexes unveil an unexpected and entirely distinct binding mode, mapping &gt;45 A away from that of any other known ACE2-using coronaviruses. Functional profiling of ACE2 orthologs from 105 mammalian species led to the identification of host tropism determinants, including an ACE2 N432-glycosylation restricting viral recognition, and the design of a soluble P.nat ACE2 mutant with potent viral neutralizing activity. Our findings reveal convergent acquisition of ACE2 usage for merbecoviruses found in European bats, underscoring the extraordinary diversity of ACE2 recognition modes among coronaviruses and the promiscuity of this receptor.

Multiple independent acquisitions of ACE2 usage in MERS-related coronaviruses.,Ma CB, Liu C, Park YJ, Tang J, Chen J, Xiong Q, Lee J, Stewart C, Asarnow D, Brown J, Tortorici MA, Yang X, Sun YH, Chen YM, Yu X, Si JY, Liu P, Tong F, Huang ML, Li J, Shi ZL, Deng Z, Veesler D, Yan H Cell. 2025 Feb 4:S0092-8674(24)01474-0. doi: 10.1016/j.cell.2024.12.031. PMID:39922191<ref>PMID:39922191</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Merbecovirus]]
[[Category: Pipistrellus nathusii]]
[[Category: Park YJ]]
[[Category: Veesler D]]