1qqp
From Proteopedia
(New page: 200px<br /><applet load="1qqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqp, resolution 1.90Å" /> '''FOOT-AND-MOUTH DISEA...) |
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| - | [[Image:1qqp.gif|left|200px]]<br /><applet load="1qqp" size=" | + | [[Image:1qqp.gif|left|200px]]<br /><applet load="1qqp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qqp, resolution 1.90Å" /> | caption="1qqp, resolution 1.90Å" /> | ||
'''FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.'''<br /> | '''FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Heparan sulfate has an important role in cell entry by foot-and-mouth | + | Heparan sulfate has an important role in cell entry by foot-and-mouth disease virus (FMDV). We find that subtype O1 FMDV binds this glycosaminoglycan with a high affinity by immobilizing a specific highly abundant motif of sulfated sugars. The binding site is a shallow depression on the virion surface, located at the junction of the three major capsid proteins, VP1, VP2 and VP3. Two pre-formed sulfate-binding sites control receptor specificity. Residue 56 of VP3, an arginine in this virus, is critical to this recognition, forming a key component of both sites. This residue is a histidine in field isolates of the virus, switching to an arginine in adaptation to tissue culture, forming the high affinity heparan sulfate-binding site. We postulate that this site is a conserved feature of FMDVs, such that in the infected animal there is a biological advantage to low affinity, or more selective, interactions with glycosaminoglycan receptors. |
==About this Structure== | ==About this Structure== | ||
| - | 1QQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. This structure | + | 1QQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. This structure supersedes the now removed PDB entry 1FHP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Abu-Ghazaleh, R.]] | [[Category: Abu-Ghazaleh, R.]] | ||
| - | [[Category: Blakemore, W | + | [[Category: Blakemore, W E.]] |
| - | [[Category: Ellard, F | + | [[Category: Ellard, F M.]] |
| - | [[Category: Fry, E | + | [[Category: Fry, E E.]] |
[[Category: Jackson, T.]] | [[Category: Jackson, T.]] | ||
| - | [[Category: King, A | + | [[Category: King, A M.Q.]] |
| - | [[Category: Lea, S | + | [[Category: Lea, S M.]] |
| - | [[Category: Newman, J | + | [[Category: Newman, J W.I.]] |
[[Category: Samuel, A.]] | [[Category: Samuel, A.]] | ||
| - | [[Category: Stuart, D | + | [[Category: Stuart, D I.]] |
[[Category: heparan sulphate]] | [[Category: heparan sulphate]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
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[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:40 2008'' |
Revision as of 12:42, 21 February 2008
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FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.
Overview
Heparan sulfate has an important role in cell entry by foot-and-mouth disease virus (FMDV). We find that subtype O1 FMDV binds this glycosaminoglycan with a high affinity by immobilizing a specific highly abundant motif of sulfated sugars. The binding site is a shallow depression on the virion surface, located at the junction of the three major capsid proteins, VP1, VP2 and VP3. Two pre-formed sulfate-binding sites control receptor specificity. Residue 56 of VP3, an arginine in this virus, is critical to this recognition, forming a key component of both sites. This residue is a histidine in field isolates of the virus, switching to an arginine in adaptation to tissue culture, forming the high affinity heparan sulfate-binding site. We postulate that this site is a conserved feature of FMDVs, such that in the infected animal there is a biological advantage to low affinity, or more selective, interactions with glycosaminoglycan receptors.
About this Structure
1QQP is a Single protein structure of sequence from Foot-and-mouth disease virus. This structure supersedes the now removed PDB entry 1FHP. Full crystallographic information is available from OCA.
Reference
The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex., Fry EE, Lea SM, Jackson T, Newman JW, Ellard FM, Blakemore WE, Abu-Ghazaleh R, Samuel A, King AM, Stuart DI, EMBO J. 1999 Feb 1;18(3):543-54. PMID:9927414
Page seeded by OCA on Thu Feb 21 14:42:40 2008
Categories: Foot-and-mouth disease virus | Single protein | Abu-Ghazaleh, R. | Blakemore, W E. | Ellard, F M. | Fry, E E. | Jackson, T. | King, A M.Q. | Lea, S M. | Newman, J W.I. | Samuel, A. | Stuart, D I. | Heparan sulphate | Icosahedral virus | Virus | Virus-receptor interactions/protein-carbohydrate interactions | Virus/viral protein
