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| | <StructureSection load='2x9m' size='340' side='right'caption='[[2x9m]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='2x9m' size='340' side='right'caption='[[2x9m]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x9m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Equine_morbillivirus Equine morbillivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x9m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hendra_henipavirus Hendra henipavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vsk|2vsk]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://proteopedia.org/fgij/fg.htm?mol=2x9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9m OCA], [http://pdbe.org/2x9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x9m RCSB], [http://www.ebi.ac.uk/pdbsum/2x9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9m ProSAT]</span></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=2x9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9m OCA], [https://pdbe.org/2x9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9m RCSB], [https://www.ebi.ac.uk/pdbsum/2x9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLYCP_HENDH GLYCP_HENDH]] Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of glycoprotein G to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). | + | [https://www.uniprot.org/uniprot/GLYCP_HENDH GLYCP_HENDH] Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of glycoprotein G to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Equine morbillivirus]] | + | [[Category: Hendra henipavirus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bowden, T A]] | + | [[Category: Bowden TA]] |
| - | [[Category: Crispin, M]] | + | [[Category: Crispin M]] |
| - | [[Category: Harvey, D]] | + | [[Category: Harvey D]] |
| - | [[Category: Jones, E Y]] | + | [[Category: Jones EY]] |
| - | [[Category: Stuart, D I]] | + | [[Category: Stuart DI]] |
| - | [[Category: Efnb2]]
| + | |
| - | [[Category: Efnb3]]
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| - | [[Category: Ephrinb2]]
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| - | [[Category: Ephrinb3]]
| + | |
| - | [[Category: Henipavirus]]
| + | |
| - | [[Category: Hnv]]
| + | |
| - | [[Category: Nipah virus]]
| + | |
| - | [[Category: Niv-g]]
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| - | [[Category: Paramyxovirus]]
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| - | [[Category: Viral attachment]]
| + | |
| - | [[Category: Viral protein]]
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| - | [[Category: Viral surface]]
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| - | [[Category: Virus envelope]]
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| Structural highlights
Function
GLYCP_HENDH Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of glycoprotein G to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hendra virus is a negative-sense single-stranded RNA virus within the Paramyxoviridae family which, together with Nipah virus, forms the Henipavirus genus. Infection with bat-borne Hendra virus leads to a disease with high mortality rates in humans. We determined the crystal structure of the unliganded six-bladed beta-propeller domain and compared it to the previously reported structure of Hendra virus attachment glycoprotein (HeV-G) in complex with its cellular receptor, ephrin-B2. As observed for the related unliganded Nipah virus structure, there is plasticity in the Glu579-Pro590 and Lys236-Ala245 ephrin-binding loops prior to receptor engagement. These data reveal that henipaviral attachment glycoproteins undergo common structural transitions upon receptor binding and further define the structural template for antihenipaviral drug design. Our analysis also provides experimental evidence for a dimeric arrangement of HeV-G that exhibits striking similarity to those observed in crystal structures of related paramyxovirus receptor-binding glycoproteins. The biological relevance of this dimer is further supported by the positional analysis of glycosylation sites from across the paramyxoviruses. In HeV-G, the sites lie away from the putative dimer interface and remain accessible to alpha-mannosidase processing on oligomerization. We therefore propose that the overall mode of dimer assembly is conserved for all paramyxoviruses; however, while the geometry of dimerization is rather closely similar for those viruses that bind flexible glycan receptors, significant (up to 60 degrees ) and different reconfigurations of the subunit packing (associated with a significant decrease in the size of the dimer interface) have accompanied the independent switching to high-affinity protein receptor binding in Hendra and measles viruses.
Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly.,Bowden TA, Crispin M, Harvey DJ, Jones EY, Stuart DI J Virol. 2010 Jun;84(12):6208-17. Epub 2010 Apr 7. PMID:20375167[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bowden TA, Crispin M, Harvey DJ, Jones EY, Stuart DI. Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly. J Virol. 2010 Jun;84(12):6208-17. Epub 2010 Apr 7. PMID:20375167 doi:10.1128/JVI.00317-10
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