6c6y: Difference between revisions

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'''Unreleased structure'''


The entry 6c6y is ON HOLD
==Crystal structure of Middle-East Respiratory Syndrome (MERS) coronavirus neutralizing antibody JC57-14 isolated from a vaccinated rhesus macaque in complex with MERS Receptor Binding Domain==
 
<StructureSection load='6c6y' size='340' side='right' caption='[[6c6y]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
Authors: Joyce, M.G., Mascola, J.R., Graham, B.S., Kwong, P.D.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6c6y]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C6Y FirstGlance]. <br>
Description: Crystal structure of Middle-East Respiratory Syndrome (MERS) coronavirus neutralizing antibody JC57-14 isolated from a vaccinated rhesus macaque in complex with MERS Receptor Binding Domain
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6c6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c6y OCA], [http://pdbe.org/6c6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c6y RCSB], [http://www.ebi.ac.uk/pdbsum/6c6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c6y ProSAT]</span></td></tr>
[[Category: Graham, B.S]]
</table>
[[Category: Joyce, M.G]]
== Function ==
[[Category: Kwong, P.D]]
[[http://www.uniprot.org/uniprot/SPIKE_CVEMC SPIKE_CVEMC]] S1 attaches the virion to the cell membrane by interacting with host DPP4, initiating the infection.<ref>PMID:23486063</ref>  S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 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 plasma cell membranes (By similarity).
[[Category: Mascola, J.R]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Graham, B S]]
[[Category: Joyce, M G]]
[[Category: Kwong, P D]]
[[Category: Mascola, J R]]
[[Category: Antibody]]
[[Category: Immune system]]
[[Category: Neutralizing]]
[[Category: Vaccine]]

Revision as of 08:08, 8 March 2018

Crystal structure of Middle-East Respiratory Syndrome (MERS) coronavirus neutralizing antibody JC57-14 isolated from a vaccinated rhesus macaque in complex with MERS Receptor Binding DomainCrystal structure of Middle-East Respiratory Syndrome (MERS) coronavirus neutralizing antibody JC57-14 isolated from a vaccinated rhesus macaque in complex with MERS Receptor Binding Domain

Structural highlights

6c6y is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPIKE_CVEMC] S1 attaches the virion to the cell membrane by interacting with host DPP4, initiating the infection.[1] S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 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 plasma cell membranes (By similarity).

References

  1. ↑ Raj VS, Mou H, Smits SL, Dekkers DH, Muller MA, Dijkman R, Muth D, Demmers JA, Zaki A, Fouchier RA, Thiel V, Drosten C, Rottier PJ, Osterhaus AD, Bosch BJ, Haagmans BL. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature. 2013 Mar 14;495(7440):251-4. doi: 10.1038/nature12005. PMID:23486063 doi:http://dx.doi.org/10.1038/nature12005

6c6y, resolution 3.32Å

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