1wnc

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{{Seed}}
 
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[[Image:1wnc.png|left|200px]]
 
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==Crystal structure of the SARS-CoV Spike protein fusion core==
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The line below this paragraph, containing "STRUCTURE_1wnc", creates the "Structure Box" on the page.
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<StructureSection load='1wnc' size='340' side='right'caption='[[1wnc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1wnc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WNC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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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=1wnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wnc OCA], [https://pdbe.org/1wnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wnc RCSB], [https://www.ebi.ac.uk/pdbsum/1wnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wnc ProSAT]</span></td></tr>
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{{STRUCTURE_1wnc| PDB=1wnc | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPIKE_SARS SPIKE_SARS] May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity.<ref>PMID:31199522</ref> Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membrane fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:14670965</ref> <ref>PMID:15496474</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]<ref>PMID:19321428</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wn/1wnc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1wnc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Severe acute respiratory syndrome coronavirus is a newly emergent virus responsible for a recent outbreak of an atypical pneumonia. The coronavirus spike protein, an enveloped glycoprotein essential for viral entry, belongs to the class I fusion proteins and is characterized by the presence of two heptad repeat (HR) regions, HR1 and HR2. These two regions are understood to form a fusion-active conformation similar to those of other typical viral fusion proteins. This hairpin structure likely juxtaposes the viral and cellular membranes, thus facilitating membrane fusion and subsequent viral entry. The fusion core protein of severe acute respiratory syndrome coronavirus spike protein was crystallized, and the structure was determined at 2.8 A of resolution. The fusion core is a six-helix bundle with three HR2 helices packed against the hydrophobic grooves on the surface of central coiled coil formed by three parallel HR1 helices in an oblique antiparallel manner. This structure shares significant similarity with the fusion core structure of mouse hepatitis virus spike protein and other viral fusion proteins, suggesting a conserved mechanism of membrane fusion. Drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation, which have been successfully used in human immunodeficiency virus 1 inhibitor development, may be applicable to the inhibition of severe acute respiratory syndrome coronavirus on the basis of structural information provided here. The relatively deep grooves on the surface of the central coiled coil will be a good target site for the design of viral fusion inhibitors.
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===Crystal structure of the SARS-CoV Spike protein fusion core===
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Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core.,Xu Y, Lou Z, Liu Y, Pang H, Tien P, Gao GF, Rao Z J Biol Chem. 2004 Nov 19;279(47):49414-9. Epub 2004 Sep 1. PMID:15345712<ref>PMID:15345712</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 1wnc" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15345712}}, adds the Publication Abstract to the page
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*[[Sandbox 3001|Sandbox 3001]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15345712 is the PubMed ID number.
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*[[Spike protein 3D structures|Spike protein 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_15345712}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1WNC is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNC OCA].
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[[Category: Large Structures]]
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[[Category: Severe acute respiratory syndrome-related coronavirus]]
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==Reference==
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[[Category: Gao GF]]
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<ref group="xtra">PMID:15345712</ref><references group="xtra"/>
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[[Category: Liu Y]]
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[[Category: Human sars coronavirus]]
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[[Category: Lou Z]]
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[[Category: Gao, G F.]]
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[[Category: Pang H]]
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[[Category: Liu, Y.]]
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[[Category: Rao Z]]
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[[Category: Lou, Z.]]
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[[Category: Tien P]]
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[[Category: Pang, H.]]
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[[Category: Xu Y]]
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[[Category: Rao, Z.]]
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[[Category: Tien, P.]]
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[[Category: Xu, Y.]]
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[[Category: Crystal structure]]
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[[Category: Fusion core]]
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[[Category: Heptad repeat]]
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[[Category: Sars-cov]]
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[[Category: Spike protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 23:05:43 2009''
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Current revision

Crystal structure of the SARS-CoV Spike protein fusion core

PDB ID 1wnc

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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