1upn
From Proteopedia
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{{Structure | {{Structure | ||
|PDB= 1upn |SIZE=350|CAPTION= <scene name='initialview01'>1upn</scene> | |PDB= 1upn |SIZE=350|CAPTION= <scene name='initialview01'>1upn</scene> | ||
| - | |SITE= <scene name='pdbsite=RB:Contributes+Over+10 | + | |SITE= <scene name='pdbsite=RB:Contributes+Over+10%+To+The+Surface+Area+Buried+Upon+Bin+...'>RB</scene> |
|LIGAND= | |LIGAND= | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1upn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upn OCA], [http://www.ebi.ac.uk/pdbsum/1upn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1upn RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
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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== | ||
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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 00:13:36 2008'' |
Revision as of 21:13, 30 March 2008
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| Sites: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A
Overview
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.
About this Structure
1UPN is a Protein complex structure of sequences from Homo sapiens and Human echovirus 11. Full crystallographic information is available from OCA.
Reference
The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55)., Bhella D, Goodfellow IG, Roversi P, Pettigrew D, Chaudhry Y, Evans DJ, Lea SM, J Biol Chem. 2004 Feb 27;279(9):8325-32. Epub 2003 Nov 21. PMID:14634014
Page seeded by OCA on Mon Mar 31 00:13:36 2008
