5NEU
Localised Reconstruction of Integrin alpha V beta 6 bound to Foot and Mouth Disease Virus O1 Manisa - Pose B.
Summary for 5NEU
| Entry DOI | 10.2210/pdb5neu/pdb |
| EMDB information | 3631 3635 |
| Descriptor | O1 Manisa VP1, O1 Manisa VP2, Capsid protein, ... (8 entities in total) |
| Functional Keywords | foot and mouth disease virus, fmdv, virus, opanasia, virus-receptor, complex |
| Biological source | Foot-and-mouth disease virus More |
| Cellular location | Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : Q6PMW3 Q6PMW3 E1ACS1 Virion : A0A1C6ZW60 Membrane; Single-pass type I membrane protein: P06756 P18564 |
| Total number of polymer chains | 6 |
| Total formula weight | 196545.22 |
| Authors | Kotecha, A.,Stuart, D. (deposition date: 2017-03-11, release date: 2017-06-21, Last modification date: 2024-11-20) |
| Primary citation | Kotecha, A.,Wang, Q.,Dong, X.,Ilca, S.L.,Ondiviela, M.,Zihe, R.,Seago, J.,Charleston, B.,Fry, E.E.,Abrescia, N.G.A.,Springer, T.A.,Huiskonen, J.T.,Stuart, D.I. Rules of engagement between alpha v beta 6 integrin and foot-and-mouth disease virus. Nat Commun, 8:15408-15408, 2017 Cited by PubMed Abstract: Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally αvβ6, 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 αvβ6 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. PubMed: 28534487DOI: 10.1038/ncomms15408 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (12.3 Å) |
Structure validation
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