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3d0g
From Proteopedia
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==Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2== | ==Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2== | ||
| - | <StructureSection load='3d0g' size='340' side='right' caption='[[3d0g]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3d0g' size='340' side='right'caption='[[3d0g]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3d0g]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3d0g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D0G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ajf|2ajf]], [[3d0h|3d0h]], [[3d0i|3d0i]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ajf|2ajf]], [[3d0h|3d0h]], [[3d0i|3d0i]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACE2 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACE2, UNQ868/PRO1885 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Angiotensin-converting_enzyme_2 Angiotensin-converting enzyme 2], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3d0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d0g OCA], [https://pdbe.org/3d0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d0g RCSB], [https://www.ebi.ac.uk/pdbsum/3d0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d0g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ACE2_PAGLA ACE2_PAGLA]] 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 (By similarity). Functional receptor for human coronavirus SARS. [[https://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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d0/3d0g_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d0/3d0g_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d0g ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3d0g" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Angiotensin-Converting Enzyme|Angiotensin-Converting Enzyme]] | *[[Angiotensin-Converting Enzyme|Angiotensin-Converting Enzyme]] | ||
| - | *[[ | + | *[[Angiotensin-Converting Enzyme 3D structures|Angiotensin-Converting Enzyme 3D structures]] |
| + | *[[Sandbox 3001|Sandbox 3001]] | ||
| + | *[[Spike protein|Spike protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Angiotensin-converting enzyme 2]] |
| - | [[Category: | + | [[Category: Human]] |
| + | [[Category: Large Structures]] | ||
[[Category: Li, F]] | [[Category: Li, F]] | ||
[[Category: Ace2]] | [[Category: Ace2]] | ||
| - | [[Category: Angiotensin-converting enzyme 2]] | ||
[[Category: Carboxypeptidase]] | [[Category: Carboxypeptidase]] | ||
[[Category: Chloride]] | [[Category: Chloride]] | ||
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[[Category: Host adaptation]] | [[Category: Host adaptation]] | ||
[[Category: Host-virus interaction]] | [[Category: Host-virus interaction]] | ||
| - | [[Category: Human]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Lipoprotein]] | [[Category: Lipoprotein]] | ||
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[[Category: Rbd]] | [[Category: Rbd]] | ||
[[Category: Receptor-binding domain]] | [[Category: Receptor-binding domain]] | ||
| + | [[Category: Sars coronavirus]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
[[Category: Spike protein]] | [[Category: Spike protein]] | ||
Current revision
Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2
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Categories: Angiotensin-converting enzyme 2 | Human | Large Structures | Li, F | Ace2 | Carboxypeptidase | Chloride | Cross-species infection | Envelope protein | Glycoprotein | Host adaptation | Host-virus interaction | Hydrolase | Lipoprotein | Membrane | Metal-binding | Metalloprotease | Palm civet | Palmitate | Protease | Rbd | Receptor-binding domain | Sars coronavirus | Secreted | Spike protein | Transmembrane | Virion | Virulence | Virus-host interface
