6m1d: Difference between revisions
New page: '''Unreleased structure''' The entry 6m1d is ON HOLD Authors: Yan, R.H., Zhang, Y.Y., Li, Y.N., Xia, L., Zhou, Q. Description: ACE2-B0AT1 complex, open conformation [[Category: Unrelea... |
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The entry | ==ACE2-B0AT1 complex, open conformation== | ||
<StructureSection load='6m1d' size='340' side='right'caption='[[6m1d]], [[Resolution|resolution]] 4.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6m1d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M1D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M1D FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLC6A19, B0AT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ACE2, UNQ868/PRO1885 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Angiotensin-converting_enzyme_2 Angiotensin-converting enzyme 2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.23 3.4.17.23] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6m1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m1d OCA], [http://pdbe.org/6m1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m1d RCSB], [http://www.ebi.ac.uk/pdbsum/6m1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m1d ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/S6A19_HUMAN S6A19_HUMAN]] Hartnup disease;Iminoglycinuria. The disease is caused by mutations affecting the gene represented in this entry. The disease may be caused by mutations affecting the gene represented in this entry. SLC6A19 deficiency combined with haploinsufficiency of SLC6A20 or partially inactivating mutations in SLC36A2, can be responsible for hyperglycinuria. The disease may be caused by mutations affecting the gene represented in this entry. SLC6A19 deficiency combined with haploinsufficiency of SLC6A20 or partially inactivating mutations in SLC36A2, can be responsible for iminoglycinuria. Additional polymorphisms and mutations in SLC6A18 can contribute to the IG phenotype in some families. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/S6A19_HUMAN S6A19_HUMAN]] Transporter that mediates resorption of neutral amino acids across the apical membrane of renal and intestinal epithelial cells (PubMed:18424768, PubMed:18484095, PubMed:19185582, PubMed:26240152). This uptake is sodium-dependent and chloride-independent (PubMed:19185582, PubMed:15286788). Requires CLTRN in kidney or ACE2 in intestine for cell surface expression and amino acid transporter activity (PubMed:19185582, PubMed:18424768).<ref>PMID:15286788</ref> <ref>PMID:18424768</ref> <ref>PMID:18484095</ref> <ref>PMID:19185582</ref> <ref>PMID:26240152</ref> [[http://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 == | |||
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a neutral amino acid transporter B(0)AT1, with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 A, with a local resolution of 3.5 A at the ACE2-RBD interface. The ACE2-B(0)AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection. | |||
Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2.,Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q Science. 2020 Mar 4. pii: science.abb2762. doi: 10.1126/science.abb2762. PMID:32132184<ref>PMID:32132184</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6m1d" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Angiotensin-converting enzyme 2]] | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Li, Y N]] | |||
[[Category: Xia, L]] | [[Category: Xia, L]] | ||
[[Category: | [[Category: Yan, R H]] | ||
[[Category: Zhang, Y | [[Category: Zhang, Y Y]] | ||
[[Category: Zhou, Q]] | [[Category: Zhou, Q]] | ||
[[Category: Ace2-b0at1 complex]] | |||
[[Category: Membrane protein]] | |||