View source for 5nej


==CryoEM Structure of Foot and Mouth Disease Virus O1 Manisa==
<SX load='5nej' size='340' side='right' viewer='molstar' caption='[[5nej]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nej]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NEJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</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=5nej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nej OCA], [https://pdbe.org/5nej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nej RCSB], [https://www.ebi.ac.uk/pdbsum/5nej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nej ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6PMW3_9PICO Q6PMW3_9PICO] 
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== Publication Abstract from PubMed ==
Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally alphavbeta6, via a conserved arginine-glycine-aspartic acid (RGD) motif in the exposed, antigenic, GH loop of capsid protein VP1. Infection can also occur in tissue culture adapted virus in the absence of integrin via acquired basic mutations interacting with heparin sulphate (HS); this virus is attenuated in natural infections. HS interaction has been visualized at a conserved site in two serotypes suggesting a propensity for sulfated-sugar binding. Here we determined the interaction between alphavbeta6 and two tissue culture adapted FMDV strains by cryo-electron microscopy. In the preferred mode of engagement, the fully open form of the integrin, hitherto unseen at high resolution, attaches to an extended GH loop via interactions with the RGD motif plus downstream hydrophobic residues. In addition, an N-linked sugar of the integrin attaches to the previously identified HS binding site, suggesting a functional role.

Rules of engagement between alphavbeta6 integrin and foot-and-mouth disease virus.,Kotecha A, Wang Q, Dong X, Ilca SL, Ondiviela M, Zihe R, Seago J, Charleston B, Fry EE, Abrescia NGA, Springer TA, Huiskonen JT, Stuart DI Nat Commun. 2017 May 23;8:15408. doi: 10.1038/ncomms15408. PMID:28534487<ref>PMID:28534487</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5nej" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
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[[Category: Foot-and-mouth disease virus]]
[[Category: Large Structures]]
[[Category: Kotecha A]]
[[Category: Stuart D]]