2c8i
From Proteopedia
(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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| - | [[Image:2c8i.gif|left|200px]]<br /> | + | [[Image:2c8i.gif|left|200px]]<br /><applet load="2c8i" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2c8i" size=" | + | |
caption="2c8i" /> | caption="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'''<br /> | '''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'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many enteroviruses bind to the complement control protein | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C8I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_25 Human echovirus 25]. Full crystallographic information is available from [http:// | + | 2C8I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_25 Human echovirus 25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bhella, D.]] | [[Category: Bhella, D.]] | ||
| - | [[Category: Evans, D | + | [[Category: Evans, D J.]] |
[[Category: Kerrigan, D.]] | [[Category: Kerrigan, D.]] | ||
| - | [[Category: Lea, S | + | [[Category: Lea, S M.]] |
| - | [[Category: Pettigrew, D | + | [[Category: Pettigrew, D M.]] |
| - | [[Category: Williams, D | + | [[Category: Williams, D T.]] |
[[Category: antigen]] | [[Category: antigen]] | ||
[[Category: blood group antigen]] | [[Category: blood group antigen]] | ||
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[[Category: virus-receptor complex]] | [[Category: virus-receptor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:06 2008'' |
Revision as of 14:46, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 16:46:06 2008
Categories: Homo sapiens | Human echovirus 25 | Protein complex | Bhella, D. | Evans, D J. | Kerrigan, D. | Lea, S M. | Pettigrew, D M. | Williams, D T. | Antigen | Blood group antigen | Cd55 | Complement pathway | Complex (virus coat/immune protein) | Daf | Echovirus | Glycoprotein | Gpi-anchor | Icosahedral virus | Immune response | Innate immunity | Lipoprotein | Picornavirus | Plasma | Polymorphism | Sushi | Virus-receptor complex
