1UPN

COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A

Summary for 1UPN

• Entry DOI: 10.2210/pdb1upn/pdb
• Related: 1H03 1H04 1H2P 1H2Q 1M11 1NWV 1OJV 1OJW 1OJY 1OK1 1OK2 1OK3 1OK9 1UOT
• EMDB information: 1057 1058
• Descriptor: ECHOVIRUS 11 COAT PROTEIN VP1, ECHOVIRUS 11 COAT PROTEIN VP2, ECHOVIRUS 11 COAT PROTEIN VP3, ... (5 entities in total)
• Functional Keywords: virus/receptor, complex (virus coat-immune protein), echovirus, picornavirus, cd55, daf, virus-receptor complex, icosahedral virus
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : Q8JKE8 Q8JKE8 Q8JKE8 Q8JKE8; Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Lipid-anchor, GPI- anchor. Isoform 3: Secreted . Isoform 4: Secreted . Isoform 5: Secreted . Isoform 6: Cell membrane ; Lipid-anchor, GPI-anchor . Isoform 7: Cell membrane ; Lipid-anchor, GPI-anchor : P08174
• Total number of polymer chains: 5
• Total formula weight: 109336.63

Authors

Bhella, D.,Goodfellow, I.G.,Roversi, P.,Pettigrew, D.,Chaudry, Y.,Evans, D.J.,Lea, S.M. (deposition date: 2003-10-08, release date: 2004-01-07, Last modification date: 2024-10-09)

Primary citation

Bhella, D.,Goodfellow, I.G.,Roversi, P.,Pettigrew, D.,Chaudhry, Y.,Evans, D.J.,Lea, S.M.
The Structure of Echovirus Type 12 Bound to a Two-Domain Fragment of its Cellular Attachment Protein Decay-Accelerating Factor (Cd 55)
J.Biol.Chem., 279:8325-, 2004

PubMed Abstract: Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decay-accelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF(34) and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virus-receptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses.

PubMed: 14634014
DOI: 10.1074/JBC.M311334200

Experimental method

ELECTRON MICROSCOPY (16 Å)