6acg - Revision history

OCA at 23:01, 10 April 2020

OCA — Fri, 10 Apr 2020 23:01:37 GMT

←Older revision		Revision as of 23:01, 10 April 2020
Line 3:		Line 3:
	<SX load='6acg' size='340' side='right' viewer='molstar' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>		<SX load='6acg' size='340' side='right' viewer='molstar' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6ACG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ACG FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE2, UNQ868/PRO1885 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg 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=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 22:
	==See Also==		==See Also==
	*[[Angiotensin-Converting Enzyme 3D structures\|Angiotensin-Converting Enzyme 3D structures]]		*[[Angiotensin-Converting Enzyme 3D structures\|Angiotensin-Converting Enzyme 3D structures]]
		+	*[[Spike protein\|Spike protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:21, 6 March 2020

OCA — Fri, 06 Mar 2020 20:21:56 GMT

←Older revision		Revision as of 20:21, 6 March 2020
Line 1:		Line 1:

	==Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1==		==Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1==
-	<~~StructureSection~~ load='6acg' size='340' side='right'caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>	+	<SX load='6acg' size='340' side='right' viewer='molstar' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>		<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>
Line 25:		Line 25:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Angiotensin-converting enzyme 2]]		[[Category: Angiotensin-converting enzyme 2]]
	[[Category: Human]]		[[Category: Human]]

OCA at 07:40, 6 November 2019

OCA — Wed, 06 Nov 2019 07:40:59 GMT

←Older revision		Revision as of 07:40, 6 November 2019
Line 1:		Line 1:

	==Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1==		==Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1==
-	<StructureSection load='6acg' size='340' side='right' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>	+	<StructureSection load='6acg' size='340' side='right'caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Cvhsa Cvhsa~~] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">~~S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA]),~~ ACE2, UNQ868/PRO1885 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg 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=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg ProSAT]</span></td></tr>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 6acg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6acg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Angiotensin-Converting Enzyme 3D structures\|Angiotensin-Converting Enzyme 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Angiotensin-converting enzyme 2]]		[[Category: Angiotensin-converting enzyme 2]]
-	[[Category: Cvhsa]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Gui, M]]		[[Category: Gui, M]]
	[[Category: Song, W]]		[[Category: Song, W]]

OCA at 06:31, 22 August 2018

OCA — Wed, 22 Aug 2018 06:31:36 GMT

←Older revision		Revision as of 06:31, 22 August 2018
Line 3:		Line 3:
	<StructureSection load='6acg' size='340' side='right' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>		<StructureSection load='6acg' size='340' side='right' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhsa Cvhsa] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA]), 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg 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=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SPIKE_CVHSA SPIKE_CVHSA]] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is 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. [[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/SPIKE_CVHSA SPIKE_CVHSA]] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is 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. [[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 ==
		+	The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.
		+
		+	Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.,Song W, Gui M, Wang X, Xiang Y PLoS Pathog. 2018 Aug 13;14(8):e1007236. doi: 10.1371/journal.ppat.1007236. PMID:30102747<ref>PMID:30102747</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6acg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 14:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Angiotensin-converting enzyme 2]]		[[Category: Angiotensin-converting enzyme 2]]
		+	[[Category: Cvhsa]]
		+	[[Category: Human]]
	[[Category: Gui, M]]		[[Category: Gui, M]]
	[[Category: Song, W]]		[[Category: Song, W]]

OCA at 21:45, 9 August 2018

OCA — Thu, 09 Aug 2018 21:45:54 GMT

←Older revision		Revision as of 21:45, 9 August 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 6acg is ON HOLD~~	+	==Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1==
-		+	<StructureSection load='6acg' size='340' side='right' caption='[[6acg]], [[Resolution\|resolution]] 5.40Å' scene=''>
-	~~Authors: Gui, M., Song, W.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6acg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACG FirstGlance]. <br>
-	~~Description:~~ Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1	+	</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>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=6acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acg OCA], [http://pdbe.org/6acg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acg RCSB], [http://www.ebi.ac.uk/pdbsum/6acg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acg ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SPIKE_CVHSA SPIKE_CVHSA]] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is 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. [[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: Gui, M]]		[[Category: Gui, M]]
	[[Category: Song, W]]		[[Category: Song, W]]
		+	[[Category: Class i fusion protein]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Membrane fusion]]
		+	[[Category: Sars-cov]]
		+	[[Category: Spike]]
		+	[[Category: Viral protein]]
		+	[[Category: Viral protein-hydrolase complex]]

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

OCA — Wed, 01 Aug 2018 16:55:51 GMT

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

←Older revision

Revision as of 16:55, 1 August 2018

OCA: New page: '''Unreleased structure''' The entry 6acg is ON HOLD Authors: Gui, M., Song, W. Description: Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound...

OCA — Wed, 01 Aug 2018 16:55:50 GMT

New page: '''Unreleased structure''' The entry 6acg is ON HOLD Authors: Gui, M., Song, W. Description: Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound...

New page

'''Unreleased structure'''

The entry 6acg is ON HOLD

Authors: Gui, M., Song, W.

Description: Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1
[[Category: Unreleased Structures]]
[[Category: Gui, M]]
[[Category: Song, W]]