2c8i
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8i OCA], [http://www.ebi.ac.uk/pdbsum/2c8i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c8i RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Blood group Cromer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=125240 125240]], Blood group, Knops system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]], CR1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]], Malaria, severe, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]], SLE susceptibility OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2C8I is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/ | + | 2C8I is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_11 Human echovirus 11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8I OCA]. |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/16272562 16272562] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16272562 16272562] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Human echovirus | + | [[Category: Human echovirus 11]] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bhella, D.]] | [[Category: Bhella, D.]] | ||
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[[Category: virus-receptor complex]] | [[Category: virus-receptor complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:55 2008'' |
Revision as of 23:17, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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.
About this Structure
2C8I is a Protein complex structure of sequences from Homo sapiens and Human echovirus 11. 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 Mon Mar 31 02:17:55 2008
Categories: Homo sapiens | Human echovirus 11 | 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
