View source for 6thb


==Receptor binding domain of the Cedar Virus attachment glycoprotein (G)==
<StructureSection load='6thb' size='340' side='right'caption='[[6thb]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6thb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cedar_virus Cedar virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6THB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=6thb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6thb OCA], [https://pdbe.org/6thb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6thb RCSB], [https://www.ebi.ac.uk/pdbsum/6thb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6thb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/J7H333_9MONO J7H333_9MONO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)-a related henipavirus that is ostensibly nonpathogenic-possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens.

A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus.,Pryce R, Azarm K, Rissanen I, Harlos K, Bowden TA, Lee B Life Sci Alliance. 2019 Dec 20;3(1). pii: 3/1/e201900578. doi:, 10.26508/lsa.201900578. Print 2020 Jan. PMID:31862858<ref>PMID:31862858</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6thb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cedar virus]]
[[Category: Large Structures]]
[[Category: Bowden T]]
[[Category: Harlos K]]
[[Category: Pryce R]]
[[Category: Rissanen I]]