Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus.
Journal, issue, pages	Nat Commun, Vol. 8, Page 15408, Year 2017
Publish date	May 23, 2017
Authors	Abhay Kotecha / Quan Wang / Xianchi Dong / Serban L Ilca / Marina Ondiviela / Rao Zihe / Julian Seago / Bryan Charleston / Elizabeth E Fry / Nicola G A Abrescia / Timothy A Springer / Juha T Huiskonen / David I Stuart /
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, ...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.
External links	Nat Commun / PubMed:28534487 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.3 - 12.3 Å
Structure data	3630 5ned EMDB-3630, PDB-5ned: CryoEM Structure of Foot and Mouth Disease Virus O PanAsia Method: EM (single particle) / Resolution: 3.1 Å 3631 5nej EMDB-3631, PDB-5nej: CryoEM Structure of Foot and Mouth Disease Virus O1 Manisa Method: EM (single particle) / Resolution: 3.1 Å 3632 5nem EMDB-3632, PDB-5nem: Localised reconstruction of alpha v beta 6 bound to Foot and Mouth Disease Virus O PanAsia - Pose A. Method: EM (single particle) / Resolution: 10.8 Å 3633 5ner EMDB-3633, PDB-5ner: Localised reconstruction of alpha v beta 6 bound to Foot and Mouth Disease Virus O PanAsia - Pose A prime. Method: EM (single particle) / Resolution: 11.5 Å 3634 5net EMDB-3634, PDB-5net: Localised Reconstruction of Integrin alpha V beta 6 bound to Foot and Mouth Disease Virus O1 Manisa - Pose A. Method: EM (single particle) / Resolution: 8.6 Å 3635 5neu EMDB-3635, PDB-5neu: Localised Reconstruction of Integrin alpha V beta 6 bound to Foot and Mouth Disease Virus O1 Manisa - Pose B. Method: EM (single particle) / Resolution: 12.3 Å PDB-5ne4: Crystal Structure of Foot and Mouth Disease Virus O PanAsia Method: X-RAY DIFFRACTION / Resolution: 2.3 Å
Chemicals	ChemComp-HOH: WATER / Water ChemComp-MAN: alpha-D-mannopyranose / Mannose ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine ChemComp-CA: Unknown entry ChemComp-MG: Unknown entry
Source	foot-and-mouth disease virus homo sapiens (human) foot-and-mouth disease virus - type o
Keywords	VIRUS / Foot and Mouth Disease Virus / FMDV / OpanAsia / virus-receptor / complex