8gry

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Current revision (09:40, 17 October 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gry OCA], [https://pdbe.org/8gry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gry RCSB], [https://www.ebi.ac.uk/pdbsum/8gry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gry ProSAT]</span></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=8gry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gry OCA], [https://pdbe.org/8gry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gry RCSB], [https://www.ebi.ac.uk/pdbsum/8gry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gry ProSAT]</span></td></tr>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/ACE2_RAT ACE2_RAT] 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. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity.[UniProtKB:Q9BYF1]
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== Publication Abstract from PubMed ==
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Multiple SARS-CoV-2 Omicron sub-variants, such as BA.2, BA.2.12.1, BA.4, and BA.5, emerge one after another. BA.5 has become the dominant strain worldwide. Additionally, BA.2.75 is significantly increasing in some countries. Exploring their receptor binding and interspecies transmission risk is urgently needed. Herein, we examine the binding capacities of human and other 28 animal ACE2 orthologs covering nine orders towards S proteins of these sub-variants. The binding affinities between hACE2 and these sub-variants remain in the range as that of previous variants of concerns (VOCs) or interests (VOIs). Notably, R493Q reverse mutation enhances the bindings towards ACE2s from humans and many animals closely related to human life, suggesting an increased risk of cross-species transmission. Structures of S/hACE2 or RBD/hACE2 complexes for these sub-variants and BA.2 S binding to ACE2 of mouse, rat or golden hamster are determined to reveal the molecular basis for receptor binding and broader interspecies recognition.
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Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants.,Zhao Z, Xie Y, Bai B, Luo C, Zhou J, Li W, Meng Y, Li L, Li D, Li X, Li X, Wang X, Sun J, Xu Z, Sun Y, Zhang W, Fan Z, Zhao X, Wu L, Ma J, Li OY, Shang G, Chai Y, Liu K, Wang P, Gao GF, Qi J Nat Commun. 2023 Jul 21;14(1):4405. doi: 10.1038/s41467-023-39942-z. PMID:37479708<ref>PMID:37479708</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8gry" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Spike protein 3D structures|Spike protein 3D structures]]
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== References ==
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<references/>
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Current revision

Cryo-EM structure of SARS-CoV-2 Omicron BA.2 RBD in complex with rat ACE2 (local refinement)

PDB ID 8gry

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