6q04

From Proteopedia

(Difference between revisions)

Current revision

MERS-CoV S structure in complex with 5-N-acetyl neuraminic acid

6q04, resolution 2.50Å

Structural highlights

6q04 is a 3 chain structure with sequence from Human betacoronavirus 2c EMC/2012. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.5Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

K0BRG7_MERS Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099] Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: 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]

Publication Abstract from PubMed

The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-Lewis(X), alpha2,3-sialyl-N-acetyl-lactosamine and alpha2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 A resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for alpha2,3-linked over alpha2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry.

Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.,Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D Nat Struct Mol Biol. 2019 Dec;26(12):1151-1157. doi: 10.1038/s41594-019-0334-7., Epub 2019 Dec 2. PMID:31792450^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors. Nat Struct Mol Biol. 2019 Dec;26(12):1151-1157. doi: 10.1038/s41594-019-0334-7., Epub 2019 Dec 2. PMID:31792450 doi:http://dx.doi.org/10.1038/s41594-019-0334-7

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6q04"

@@ Line 3: / Line 3: @@
 <SX load='6q04' size='340' side='right' viewer='molstar' caption='[[6q04]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6q04]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_betacoronavirus_2c_emc/2012 Human betacoronavirus 2c emc/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q04 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Q04 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6q04]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betacoronavirus_2c_EMC/2012 Human betacoronavirus 2c EMC/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q04 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5&#8491;</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=6q04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q04 OCA], [http://pdbe.org/6q04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q04 RCSB], [http://www.ebi.ac.uk/pdbsum/6q04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q04 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=6q04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q04 OCA], [https://pdbe.org/6q04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q04 RCSB], [https://www.ebi.ac.uk/pdbsum/6q04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q04 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/K0BRG7_MERS K0BRG7_MERS] Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099]  Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099]  Spike protein S2: 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]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 21: @@
 ==See Also==
-*[[Spike protein|Spike protein]]
+*[[Sandbox 3001|Sandbox 3001]]
+*[[Spike protein 3D structures|Spike protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Human betacoronavirus 2c emc/2012]]
+[[Category: Human betacoronavirus 2c EMC/2012]]
 [[Category: Large Structures]]
-[[Category: Bosch, B J]]
+[[Category: Bosch BJ]]
-[[Category: DiMaio, F D]]
+[[Category: DiMaio FD]]
-[[Category: Li, W]]
+[[Category: Li W]]
-[[Category: Park, Y J]]
+[[Category: Park YJ]]
-[[Category: Structural genomic]]
+[[Category: Sauer M]]
-[[Category: Sauer, M]]
+[[Category: Tortorici MA]]
-[[Category: Tortorici, M A]]
+[[Category: Veesler D]]
-[[Category: Veesler, D]]
+[[Category: Walls AC]]
-[[Category: Walls, A C]]
+[[Category: Wang Z]]
-[[Category: Wang, Z]]
-[[Category: Coronavirus]]
-[[Category: Membrane fusion]]
-[[Category: Mers-cov]]
-[[Category: Spike glycoprotein]]
-[[Category: Ssgcid]]
-[[Category: Viral protein]]

6q04

From Proteopedia

Current revision

MERS-CoV S structure in complex with 5-N-acetyl neuraminic acid

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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