2qzd: Difference between revisions

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==Overview==
==Overview==
Many entero-, parecho-, and rhinoviruses use IgG-like receptors that bind, into the viral canyon and are required to initiate viral uncoating during, infection. However, some of these viruses use an alternative or additional, receptor that binds outside the canyon. Both the coxsackievirus-adenovirus, receptor (CAR), an IgG-like molecule that binds into the viral canyon, and, decay-accelerating factor (DAF) have been identified as cellular receptors, for coxsackievirus B3 (CVB3). A cryo-electron microscopy reconstruction of, a variant of CVB3 complexed with DAF shows full occupancy of the DAF, receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete, with one another. The binding site of DAF on CVB3 differs from the binding, site of DAF on the surface of echoviruses, suggesting independent, evolutionary processes.
Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes.
 
==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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==Reference==
==Reference==
The Interaction of Decay-accelerating Factor with Coxsackievirus B3., Hafenstein S, Bowman VD, Chipman PR, Kelly CM, Lin F, Medof DE, Rossmann MG, J Virol. 2007 Sep 5;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17804498 17804498]
Interaction of decay-accelerating factor with coxsackievirus B3., Hafenstein S, Bowman VD, Chipman PR, Bator Kelly CM, Lin F, Medof ME, Rossmann MG, J Virol. 2007 Dec;81(23):12927-35. Epub 2007 Sep 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17804498 17804498]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bowman, V.D.]]
[[Category: Bowman, V D.]]
[[Category: Chipman, P.R.]]
[[Category: Chipman, P R.]]
[[Category: Hafenstein, S.]]
[[Category: Hafenstein, S.]]
[[Category: Kelly, C.M.Bator.]]
[[Category: Kelly, C M.Bator.]]
[[Category: Lin, F.]]
[[Category: Lin, F.]]
[[Category: Medof, M.E.]]
[[Category: Medof, M E.]]
[[Category: Rossmann, M.G.]]
[[Category: Rossmann, M G.]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
[[Category: blood group antigen]]
[[Category: blood group antigen]]
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[[Category: sushi]]
[[Category: sushi]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:27 2008''

Revision as of 19:43, 21 February 2008

File:2qzd.gif


2qzd

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Fitted structure of SCR4 of DAF into cryoEM density

OverviewOverview

Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes.

DiseaseDisease

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 StructureAbout this Structure

2QZD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Interaction of decay-accelerating factor with coxsackievirus B3., Hafenstein S, Bowman VD, Chipman PR, Bator Kelly CM, Lin F, Medof ME, Rossmann MG, J Virol. 2007 Dec;81(23):12927-35. Epub 2007 Sep 5. PMID:17804498

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