6p72

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m (Protected "6p72" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6p72 is ON HOLD
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==Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein global domain==
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<StructureSection load='6p72' size='340' side='right'caption='[[6p72]], [[Resolution|resolution]] 3.28&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6p72]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cedpv Cedpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P72 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P72 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<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=6p72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p72 OCA], [http://pdbe.org/6p72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p72 RCSB], [http://www.ebi.ac.uk/pdbsum/6p72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p72 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only approximately 30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.
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Authors:
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Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.,Laing ED, Navaratnarajah CK, Cheliout Da Silva S, Petzing SR, Xu Y, Sterling SL, Marsh GA, Wang LF, Amaya M, Nikolov DB, Cattaneo R, Broder CC, Xu K Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715. doi:, 10.1073/pnas.1911773116. Epub 2019 Sep 23. PMID:31548390<ref>PMID:31548390</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6p72" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cedpv]]
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[[Category: Large Structures]]
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[[Category: Nikolov, D B]]
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[[Category: Xu, K]]
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[[Category: Xu, Y]]
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[[Category: Attachment]]
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[[Category: Cedar virus]]
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[[Category: Glycoprotein]]
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[[Category: Viral protein]]

Revision as of 06:16, 10 October 2019

Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein global domain

PDB ID 6p72

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