2beq

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[[Image:2beq.gif|left|200px]]
 
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==Structure of a Proteolytically Resistant Core from the Severe Acute Respiratory Syndrome Coronavirus S2 Fusion Protein==
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The line below this paragraph, containing "STRUCTURE_2beq", creates the "Structure Box" on the page.
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<StructureSection load='2beq' size='340' side='right'caption='[[2beq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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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'>[[2beq]] 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=2BEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BEQ FirstGlance]. <br>
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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]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_2beq| PDB=2beq | SCENE= }}
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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=2beq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2beq OCA], [https://pdbe.org/2beq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2beq RCSB], [https://www.ebi.ac.uk/pdbsum/2beq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2beq ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF A PROTEOLYTICALLY RESISTANT CORE FROM THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS S2 FUSION PROTEIN'''
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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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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/be/2beq_consurf.spt"</scriptWhenChecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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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=2beq ConSurf].
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<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
A coronavirus (CoV) has recently been identified as the causative agent of the severe acute respiratory syndrome (SARS) in humans. CoVs enter target cells through fusion of viral and cellular membranes mediated by the viral envelope glycoprotein S. We have determined by x-ray crystallography the structure of a proteolytically stable core fragment from the heptad repeat (HR) regions HR1 and HR2 of the SARS-CoV S protein. We have also determined the structure of an HR1-HR2 S core fragment, containing a shorter HR1 peptide and a C-terminally longer HR2 peptide that extends up to the transmembrane region. In these structures, three HR1 helices form a parallel coiled-coil trimer, whereas three HR2 peptides pack in an oblique and antiparallel fashion into the coiled-coil hydrophobic grooves, adopting mixed extended and alpha-helical conformations as in postfusion paramyxoviruses F proteins structures. Our structure positions a previously proposed internal fusion peptide adjacent to the N-terminus of HR1. Peptides from the HR2 region of SARS-CoV S have been shown to inhibit viral entry and infection in vitro. The structures presented here can thus open the path to the design of small-molecule inhibitors of viral entry and candidate vaccine antigens against this virus.
A coronavirus (CoV) has recently been identified as the causative agent of the severe acute respiratory syndrome (SARS) in humans. CoVs enter target cells through fusion of viral and cellular membranes mediated by the viral envelope glycoprotein S. We have determined by x-ray crystallography the structure of a proteolytically stable core fragment from the heptad repeat (HR) regions HR1 and HR2 of the SARS-CoV S protein. We have also determined the structure of an HR1-HR2 S core fragment, containing a shorter HR1 peptide and a C-terminally longer HR2 peptide that extends up to the transmembrane region. In these structures, three HR1 helices form a parallel coiled-coil trimer, whereas three HR2 peptides pack in an oblique and antiparallel fashion into the coiled-coil hydrophobic grooves, adopting mixed extended and alpha-helical conformations as in postfusion paramyxoviruses F proteins structures. Our structure positions a previously proposed internal fusion peptide adjacent to the N-terminus of HR1. Peptides from the HR2 region of SARS-CoV S have been shown to inhibit viral entry and infection in vitro. The structures presented here can thus open the path to the design of small-molecule inhibitors of viral entry and candidate vaccine antigens against this virus.
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==About this Structure==
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Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein.,Supekar VM, Bruckmann C, Ingallinella P, Bianchi E, Pessi A, Carfi A Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63. Epub 2004 Dec 16. PMID:15604146<ref>PMID:15604146</ref>
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2BEQ is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein., Supekar VM, Bruckmann C, Ingallinella P, Bianchi E, Pessi A, Carfi A, Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63. Epub 2004 Dec 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15604146 15604146]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2beq" style="background-color:#fffaf0;"></div>
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[[Category: Bianchi, E.]]
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== References ==
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[[Category: Bruckmann, C.]]
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<references/>
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[[Category: Carfi, A.]]
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__TOC__
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[[Category: Ingallinella, P.]]
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</StructureSection>
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[[Category: Pessi, A.]]
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[[Category: Large Structures]]
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[[Category: Supekar, V M.]]
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[[Category: Severe acute respiratory syndrome-related coronavirus]]
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[[Category: Coiled coil]]
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[[Category: Bianchi E]]
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[[Category: Envelope protein]]
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[[Category: Bruckmann C]]
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[[Category: Glycoprotein]]
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[[Category: Carfi A]]
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[[Category: Membrane fusion]]
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[[Category: Ingallinella P]]
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[[Category: Sar]]
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[[Category: Pessi A]]
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[[Category: Signal]]
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[[Category: Supekar VM]]
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[[Category: Transmembrane]]
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[[Category: Viral entry]]
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[[Category: Virulence]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:11:29 2008''
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Current revision

Structure of a Proteolytically Resistant Core from the Severe Acute Respiratory Syndrome Coronavirus S2 Fusion Protein

PDB ID 2beq

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