2C8I

Complex Of Echovirus Type 12 With Domains 1, 2, 3 and 4 Of Its Receptor Decay Accelerating Factor (Cd55) By Cryo Electron Microscopy At 16 A

Summary for 2C8I

• Entry DOI: 10.2210/pdb2c8i/pdb
• Related: 1H03 1H04 1H2P 1H2Q 1M11 1NWV 1OJV 1OJW 1OJY 1OK1 1OK2 1OK3 1OK9 1UOT 1UPN
• EMDB information: 1182 1183
• Descriptor: ECHOVIRUS 11 COAT PROTEIN VP1, ECHOVIRUS 11 COAT PROTEIN VP2, ECHOVIRUS 11 COAT PROTEIN VP3, ... (5 entities in total)
• Functional Keywords: picornavirus, daf, virus-receptor complex, antigen, blood group antigen, complement pathway, gpi-anchor, immune response, innate immunity, lipoprotein, plasma, sushi, virus/receptor
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Capsid protein VP0: Virion . Capsid protein VP4: Virion . Capsid protein VP2: Virion . Capsid protein VP3: Virion . Capsid protein VP1: Virion . Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion . Protease 3C: Host cytoplasm . Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P29813 P29813 P29813 P29813; 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: 127995.66

Authors

Pettigrew, D.M.,Williams, D.T.,Kerrigan, D.,Evans, D.J.,Lea, S.M.,Bhella, D. (deposition date: 2005-12-05, release date: 2006-01-17, Last modification date: 2024-05-08)

Primary citation

Pettigrew, D.M.,Williams, D.T.,Kerrigan, D.,Evans, D.J.,Lea, S.M.,Bhella, D.
Structural and Functional Insights Into the Interaction of Echoviruses and Decay-Accelerating Factor.
J.Biol.Chem., 281:5169-, 2006

PubMed Abstract: Many enteroviruses bind to the complement control protein decay-accelerating factor (DAF) to facilitate cell entry. We present here a structure for echovirus (EV) type 12 bound to DAF using cryo-negative stain transmission electron microscopy and three-dimensional image reconstruction to 16-A resolution, which we interpreted using the atomic structures of EV11 and DAF. DAF binds to a hypervariable region of the capsid close to the 2-fold symmetry axes in an interaction that involves mostly the short consensus repeat 3 domain of DAF and the capsid protein VP2. A bulge in the density for the short consensus repeat 3 domain suggests that a loop at residues 174-180 rearranges to prevent steric collision between closely packed molecules at the 2-fold symmetry axes. Detailed analysis of receptor interactions between a variety of echoviruses and DAF using surface plasmon resonance and comparison of this structure (and our previous work; Bhella, D., Goodfellow, I. G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D. J., and Lea, S. M. (2004) J. Biol. Chem. 279, 8325-8332) with reconstructions published for EV7 bound to DAF support major differences in receptor recognition among these viruses. However, comparison of the electron density for the two virus.receptor complexes (rather than comparisons of the pseudo-atomic models derived from fitting the coordinates into these densities) suggests that the dramatic differences in interaction affinities/specificities may arise from relatively subtle structural differences rather than from large-scale repositioning of the receptor with respect to the virus surface.

PubMed: 16272562
DOI: 10.1074/JBC.M510362200

Experimental method

ELECTRON MICROSCOPY (14 Å)