1qqp: Difference between revisions

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[[Image:1qqp.gif|left|200px]]
{{Seed}}
[[Image:1qqp.png|left|200px]]


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{{STRUCTURE_1qqp|  PDB=1qqp  |  SCENE=  }}  
{{STRUCTURE_1qqp|  PDB=1qqp  |  SCENE=  }}  


'''FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.'''
===FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9927414}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9927414 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9927414}}


==About this Structure==
==About this Structure==
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[[Category: Virus-receptor interactions/protein-carbohydrate interaction]]
[[Category: Virus-receptor interactions/protein-carbohydrate interaction]]
[[Category: Virus/viral protein]]
[[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 Tue Jul 29 08:12:49 2008''
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