1upn: Difference between revisions
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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. | ||
==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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:37:26 2007'' | ||
