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1qqp
From Proteopedia
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[[Image:1qqp.gif|left|200px]] | [[Image:1qqp.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1qqp| PDB=1qqp | SCENE= }} | |
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'''FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.''' | '''FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QQP is a [[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 | + | 1QQP is a [[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 [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1fhp 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: Samuel, A.]] | [[Category: Samuel, A.]] | ||
[[Category: Stuart, D I.]] | [[Category: Stuart, D I.]] | ||
| - | [[Category: | + | [[Category: Heparan sulphate]] |
| - | [[Category: | + | [[Category: Icosahedral virus]] |
| - | [[Category: | + | [[Category: Virus]] |
| - | [[Category: | + | [[Category: Virus-receptor interactions/protein-carbohydrate interaction]] |
| - | [[Category: | + | [[Category: Virus/viral protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:35:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:35, 3 May 2008
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 Sat May 3 06:35:43 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 interaction | Virus/viral protein
