1dgi
From Proteopedia
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|PDB= 1dgi |SIZE=350|CAPTION= <scene name='initialview01'>1dgi</scene>, resolution 22.0Å | |PDB= 1dgi |SIZE=350|CAPTION= <scene name='initialview01'>1dgi</scene>, resolution 22.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MYR:MYRISTIC ACID'>MYR</scene> | + | |LIGAND= <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2plv|2PLV]], [[1neu|1NEU]], [[1cic|1CIC]], [[1bih|1BIH]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgi OCA], [http://www.ebi.ac.uk/pdbsum/1dgi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dgi RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype 1) has been determined to 22-A resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection. | The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype 1) has been determined to 22-A resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Polio, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173850 173850]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Rossmann, M G.]] | [[Category: Rossmann, M G.]] | ||
[[Category: Wimmer, E.]] | [[Category: Wimmer, E.]] | ||
| - | [[Category: MYR]] | ||
[[Category: cd155]] | [[Category: cd155]] | ||
[[Category: cryo-electron microscopy]] | [[Category: cryo-electron microscopy]] | ||
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[[Category: pvr]] | [[Category: pvr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:13 2008'' |
Revision as of 16:41, 30 March 2008
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| , resolution 22.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 2PLV, 1NEU, 1CIC, 1BIH
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cryo-EM structure of human poliovirus(serotype 1)complexed with three domain CD155
Overview
The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype 1) has been determined to 22-A resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection.
About this Structure
1DGI is a Protein complex structure of sequences from Homo sapiens and Human poliovirus 1. The following page contains interesting information on the relation of 1DGI with [Poliovirus and Rhinovirus]. Full crystallographic information is available from OCA.
Reference
Interaction of the poliovirus receptor with poliovirus., He Y, Bowman VD, Mueller S, Bator CM, Bella J, Peng X, Baker TS, Wimmer E, Kuhn RJ, Rossmann MG, Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):79-84. PMID:10618374
Page seeded by OCA on Sun Mar 30 19:41:13 2008
Categories: Homo sapiens | Human poliovirus 1 | Poliovirus and Rhinovirus | Protein complex | Baker, T S. | Bator, C M. | Bella, J. | Bowman, V D. | He, Y. | Kuhn, R J. | Mueller, S. | Peng, X. | Rossmann, M G. | Wimmer, E. | Cd155 | Cryo-electron microscopy | Human poliovirus | Icosahedral virus | Poliovirus-receptor complex | Pvr
