2c8i

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(New page: 200px<br /> <applet load="2c8i" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c8i" /> '''COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 1...)
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Revision as of 19:06, 12 November 2007


2c8i

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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

Contents

Overview

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.

Disease

Known diseases associated with this structure: Blood group Cromer OMIM:[125240], Blood group, Knops system OMIM:[120620], CR1 deficiency OMIM:[120620], Malaria, severe, resistance to OMIM:[120620], SLE susceptibility OMIM:[120620]

About this Structure

2C8I is a Protein complex structure of sequences from Homo sapiens and Human echovirus 25. Full crystallographic information is available from OCA.

Reference

Structural and functional insights into the interaction of echoviruses and decay-accelerating factor., Pettigrew DM, Williams DT, Kerrigan D, Evans DJ, Lea SM, Bhella D, J Biol Chem. 2006 Feb 24;281(8):5169-77. Epub 2005 Nov 4. PMID:16272562

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