8iov: Difference between revisions

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'''Unreleased structure'''


The entry 8iov is ON HOLD  until Paper Publication
==Structure of SARS-CoV-2 XBB.1 spike RBD in complex with ACE2==
<StructureSection load='8iov' size='340' side='right'caption='[[8iov]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8iov]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=8IOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IOV 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]] 3.29&#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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=8iov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iov OCA], [https://pdbe.org/8iov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iov RCSB], [https://www.ebi.ac.uk/pdbsum/8iov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iov ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACE2_HUMAN ACE2_HUMAN] Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.<ref>PMID:10969042</ref> <ref>PMID:10924499</ref> <ref>PMID:14647384</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In late 2022, SARS-CoV-2 Omicron subvariants have become highly diversified, and XBB is spreading rapidly around the world. Our phylogenetic analyses suggested that XBB emerged through the recombination of two cocirculating BA.2 lineages, BJ.1 and BM.1.1.1 (a progeny of BA.2.75), during the summer of 2022. XBB.1 is the variant most profoundly resistant to BA.2/5 breakthrough infection sera to date and is more fusogenic than BA.2.75. The recombination breakpoint is located in the receptor-binding domain of spike, and each region of the recombinant spike confers immune evasion and increases fusogenicity. We further provide the structural basis for the interaction between XBB.1 spike and human ACE2. Finally, the intrinsic pathogenicity of XBB.1 in male hamsters is comparable to or even lower than that of BA.2.75. Our multiscale investigation provides evidence suggesting that XBB is the first observed SARS-CoV-2 variant to increase its fitness through recombination rather than substitutions.


Authors: Anraku, Y., Kita, S., Yajima, H., Sasaki, J., Sasaki-Tabata, K., Maenaka, K., Hashiguchi, T.
Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants.,Tamura T, Ito J, Uriu K, Zahradnik J, Kida I, Anraku Y, Nasser H, Shofa M, Oda Y, Lytras S, Nao N, Itakura Y, Deguchi S, Suzuki R, Wang L, Begum MM, Kita S, Yajima H, Sasaki J, Sasaki-Tabata K, Shimizu R, Tsuda M, Kosugi Y, Fujita S, Pan L, Sauter D, Yoshimatsu K, Suzuki S, Asakura H, Nagashima M, Sadamasu K, Yoshimura K, Yamamoto Y, Nagamoto T, Schreiber G, Maenaka K, Hashiguchi T, Ikeda T, Fukuhara T, Saito A, Tanaka S, Matsuno K, Takayama K, Sato K Nat Commun. 2023 May 16;14(1):2800. doi: 10.1038/s41467-023-38435-3. PMID:37193706<ref>PMID:37193706</ref>


Description: Structure of SARS-CoV-2 XBB.1 spike RBD in complex with ACE2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hashiguchi, T]]
<div class="pdbe-citations 8iov" style="background-color:#fffaf0;"></div>
[[Category: Sasaki, J]]
== References ==
[[Category: Anraku, Y]]
<references/>
[[Category: Yajima, H]]
__TOC__
[[Category: Sasaki-Tabata, K]]
</StructureSection>
[[Category: Kita, S]]
[[Category: Homo sapiens]]
[[Category: Maenaka, K]]
[[Category: Large Structures]]
[[Category: Severe acute respiratory syndrome coronavirus 2]]
[[Category: Anraku Y]]
[[Category: Hashiguchi T]]
[[Category: Kita S]]
[[Category: Maenaka K]]
[[Category: Sasaki J]]
[[Category: Sasaki-Tabata K]]
[[Category: Yajima H]]

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