4l3n

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus

Structural highlights

4l3n is a 2 chain structure with sequence from Human betacoronavirus 2c Jordan-N3/2012. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.13Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

M4SVE7_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 newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people with a fatality rate of more than 50%. Alarmingly, the virus demonstrates a capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents the structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans.

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.,Chen Y, Rajashankar KR, Yang Y, Agnihothram SS, Liu C, Lin YL, Baric RS, Li F J Virol. 2013 Jul 31. PMID:23903833^[1]

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

References

↑ Chen Y, Rajashankar KR, Yang Y, Agnihothram SS, Liu C, Lin YL, Baric RS, Li F. Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus. J Virol. 2013 Jul 31. PMID:23903833 doi:10.1128/JVI.01756-13

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4l3n"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4l3n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betacoronavirus_2c_Jordan-N3/2012 Human betacoronavirus 2c Jordan-N3/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L3N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l3n OCA], [https://pdbe.org/4l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l3n RCSB], [https://www.ebi.ac.uk/pdbsum/4l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l3n ProSAT]</span></td></tr>
 </table>

4l3n

From Proteopedia

Current revision

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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