6m17 - Revision history

OCA at 17:46, 10 March 2021

OCA — Wed, 10 Mar 2021 17:46:23 GMT

OCA at 07:31, 4 November 2020

OCA — Wed, 04 Nov 2020 07:31:56 GMT

←Older revision		Revision as of 07:31, 4 November 2020
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	<SX load='6m17' size='340' side='right' viewer='molstar' caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>		<SX load='6m17' size='340' side='right' viewer='molstar' caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human Human~~] and [http://en.wikipedia.org/wiki/~~Wcpv Wcpv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/2019-ncov 2019-ncov] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]), S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 ~~WCPV~~])</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]), S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</span></td></tr>
	</table>		</table>
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	</div>		</div>
	<div class="pdbe-citations 6m17" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6m17" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Angiotensin-Converting Enzyme 3D structures\|Angiotensin-Converting Enzyme 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</SX>		</SX>
		+	[[Category: 2019-ncov]]
	[[Category: Human]]		[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Wcpv]]
	[[Category: Guo, Y Y]]		[[Category: Guo, Y Y]]
	[[Category: Li, Y N]]		[[Category: Li, Y N]]

OCA at 06:28, 6 May 2020

OCA — Wed, 06 May 2020 06:28:48 GMT

←Older revision		Revision as of 06:28, 6 May 2020
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	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='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]), S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 WCPV])</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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</span></td></tr>
	</table>		</table>
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	[[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.		[[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 ==		== 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>	+	[[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/SPIKE_SARS2 SPIKE_SARS2]] attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:32075877</ref> <ref>PMID:32142651</ref> <ref>PMID:32155444</ref> mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] [[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: Angiotensin-converting enzyme 2]]
	[[Category: Human]]		[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 05:24, 15 April 2020

OCA — Wed, 15 Apr 2020 05:24:36 GMT

←Older revision		Revision as of 05:24, 15 April 2020
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	==The 2019-nCoV RBD/ACE2-B0AT1 complex==		==The 2019-nCoV RBD/ACE2-B0AT1 complex==
-	<~~StructureSection~~ load='6m17' size='340' side='right'caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<SX load='6m17' size='340' side='right' viewer='molstar' caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
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	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Angiotensin-converting enzyme 2]]		[[Category: Angiotensin-converting enzyme 2]]
	[[Category: Human]]		[[Category: Human]]

OCA at 07:18, 8 April 2020

OCA — Wed, 08 Apr 2020 07:18:32 GMT

←Older revision		Revision as of 07:18, 8 April 2020
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	<StructureSection load='6m17' size='340' side='right'caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='6m17' size='340' side='right'caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6M17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='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='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://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 10:19, 18 March 2020

OCA — Wed, 18 Mar 2020 10:19:40 GMT

←Older revision		Revision as of 10:19, 18 March 2020
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	<StructureSection load='6m17' size='340' side='right'caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='6m17' size='340' side='right'caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6M17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</span></td></tr>
Line 12:		Line 13:
	== Function ==		== 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>		[[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>
		+	</div>
		+	<div class="pdbe-citations 6m17" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 17:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Angiotensin-converting enzyme 2]]		[[Category: Angiotensin-converting enzyme 2]]
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Wcpv]]
	[[Category: Guo, Y Y]]		[[Category: Guo, Y Y]]
	[[Category: Li, Y N]]		[[Category: Li, Y N]]

OCA at 07:21, 11 March 2020

OCA — Wed, 11 Mar 2020 07:21:02 GMT

←Older revision		Revision as of 07:21, 11 March 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 6m17 ~~is ON HOLD~~	+	==The 2019-nCoV RBD/ACE2-B0AT1 complex==
-		+	<StructureSection load='6m17' size='340' side='right'caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~Authors~~: ~~Yan, R~~.H., ~~Zhang~~, Y.Y., Li, Y.N., ~~Xia~~, L., ~~Guo~~, Y.Y., ~~Zhou~~, Q.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
-	~~Description~~: ~~The 2019-nCoV RBD~~/ACE2-~~B0AT1 complex~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [http://pdbe.org/6m17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [http://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Angiotensin-converting enzyme 2]]
		+	[[Category: Large Structures]]
		+	[[Category: Guo, Y Y]]
		+	[[Category: Li, Y N]]
	[[Category: Xia, L]]		[[Category: Xia, L]]
-	[[Category: Li, ~~Y.N]]~~	+	[[Category: Yan, R H]]
-	~~[[Category: Guo, Y.Y~~]]	+	[[Category: Zhang, Y Y]]
-	[[Category: Zhang, Y.Y]]	+
-	~~[[Category: Yan, R.H~~]]	+
	[[Category: Zhou, Q]]		[[Category: Zhou, Q]]
		+	[[Category: 2019-ncov rbd]]
		+	[[Category: Ace2-b0at1 complex]]
		+	[[Category: Membrane protein]]
		+	[[Category: Membrane protein-viral protein complex]]

OCA: Protected "6m17" [edit=sysop:move=sysop]

OCA — Wed, 04 Mar 2020 05:29:08 GMT

Protected "6m17" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:29, 4 March 2020

OCA: New page: '''Unreleased structure''' The entry 6m17 is ON HOLD Authors: Yan, R.H., Zhang, Y.Y., Li, Y.N., Xia, L., Guo, Y.Y., Zhou, Q. Description: The 2019-nCoV RBD/ACE2-B0AT1 complex [[Categor...

OCA — Wed, 04 Mar 2020 05:29:07 GMT

New page: '''Unreleased structure''' The entry 6m17 is ON HOLD Authors: Yan, R.H., Zhang, Y.Y., Li, Y.N., Xia, L., Guo, Y.Y., Zhou, Q. Description: The 2019-nCoV RBD/ACE2-B0AT1 complex [[Categor...

New page

'''Unreleased structure'''

The entry 6m17 is ON HOLD

Authors: Yan, R.H., Zhang, Y.Y., Li, Y.N., Xia, L., Guo, Y.Y., Zhou, Q.

Description: The 2019-nCoV RBD/ACE2-B0AT1 complex
[[Category: Unreleased Structures]]
[[Category: Xia, L]]
[[Category: Li, Y.N]]
[[Category: Guo, Y.Y]]
[[Category: Zhang, Y.Y]]
[[Category: Yan, R.H]]
[[Category: Zhou, Q]]

←Older revision		Revision as of 17:46, 10 March 2021
Line 3:		Line 3:
	<SX load='6m17' size='340' side='right' viewer='molstar' caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>		<SX load='6m17' size='340' side='right' viewer='molstar' caption='[[6m17]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/2019-ncov 2019-ncov] and [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6m17]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/2019-ncov 2019-ncov] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M17 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]), S, 2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SLC6A19, B0AT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ACE2, UNQ868/PRO1885 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), S, 2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [~~http~~://pdbe.org/6m17 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 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=6m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m17 OCA], [https://pdbe.org/6m17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m17 RCSB], [https://www.ebi.ac.uk/pdbsum/6m17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m17 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== 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.	+	[[https://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 ==		== 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/SPIKE_SARS2 SPIKE_SARS2]] attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:32075877</ref> <ref>PMID:32142651</ref> <ref>PMID:32155444</ref> mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] [[~~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>	+	[[https://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> [[https://www.uniprot.org/uniprot/SPIKE_SARS2 SPIKE_SARS2]] attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:32075877</ref> <ref>PMID:32142651</ref> <ref>PMID:32155444</ref> mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] [[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==