8dm9: Difference between revisions

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'''Unreleased structure'''


The entry 8dm9 is ON HOLD  until Paper Publication
==Cryo-EM structure of SARS-CoV-2 Omicron BA.1 spike protein in complex with mouse ACE2==
<StructureSection load='8dm9' size='340' side='right'caption='[[8dm9]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8dm9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DM9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8dm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dm9 OCA], [https://pdbe.org/8dm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dm9 RCSB], [https://www.ebi.ac.uk/pdbsum/8dm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dm9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACE2_MOUSE ACE2_MOUSE] Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A (By similarity). By cleavage of angiotensin II, may be an important regulator of heart function (PubMed:12075344, PubMed:12967627). By cleavage of angiotensin II, may also have a protective role in acute lung injury (PubMed:16001071). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19, regulating its trafficking on the cell surface and its activity (PubMed:19185582, PubMed:18424768, PubMed:22677001).[UniProtKB:Q9BYF1]<ref>PMID:12075344</ref> <ref>PMID:12967627</ref> <ref>PMID:16001071</ref> <ref>PMID:18424768</ref> <ref>PMID:19185582</ref> <ref>PMID:22677001</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The BA.2 sub-lineage of the Omicron (B.1.1.529) severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant rapidly supplanted the original BA.1 sub-lineage in early 2022. Both lineages threatened the efficacy of vaccine-elicited antibodies and acquired increased binding to several mammalian ACE2 receptors. Cryoelectron microscopy (cryo-EM) analysis of the BA.2 spike (S) glycoprotein in complex with mouse ACE2 (mACE2) identifies BA.1- and BA.2-mutated residues Q493R, N501Y, and Y505H as complementing non-conserved residues between human and mouse ACE2, rationalizing the enhanced S protein-mACE2 interaction for Omicron variants. Cryo-EM structures of the BA.2 S-human ACE2 complex and of the extensively mutated BA.2 amino-terminal domain (NTD) reveal a dramatic reorganization of the highly antigenic N1 loop into a beta-strand, providing an explanation for decreased binding of the BA.2 S protein to antibodies isolated from BA.1-convalescent patients. Our analysis reveals structural mechanisms underlying the antigenic drift in the rapidly evolving Omicron variant landscape.


Authors: Zhu, X., Saville, J.W., Mannar, D., Berezuk, A.M., Cholak, S., Tuttle, K.S., Vahdatihassani, F., Subramaniam, S.
Structural analysis of receptor engagement and antigenic drift within the BA.2 spike protein.,Saville JW, Mannar D, Zhu X, Berezuk AM, Cholak S, Tuttle KS, Vahdatihassani F, Subramaniam S Cell Rep. 2023 Jan 4;42(1):111964. doi: 10.1016/j.celrep.2022.111964. PMID:36640338<ref>PMID:36640338</ref>


Description: Cryo-EM structure of SARS-CoV-2 Omicron BA.1 spike protein in complex with mouse ACE2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Subramaniam, S]]
<div class="pdbe-citations 8dm9" style="background-color:#fffaf0;"></div>
[[Category: Zhu, X]]
== References ==
[[Category: Tuttle, K.S]]
<references/>
[[Category: Mannar, D]]
__TOC__
[[Category: Saville, J.W]]
</StructureSection>
[[Category: Vahdatihassani, F]]
[[Category: Large Structures]]
[[Category: Cholak, S]]
[[Category: Mus musculus]]
[[Category: Berezuk, A.M]]
[[Category: Severe acute respiratory syndrome coronavirus 2]]
[[Category: Berezuk AM]]
[[Category: Cholak S]]
[[Category: Mannar D]]
[[Category: Saville JW]]
[[Category: Subramaniam S]]
[[Category: Tuttle KS]]
[[Category: Vahdatihassani F]]
[[Category: Zhu X]]
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