1qqp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1qqp |SIZE=350|CAPTION= <scene name='initialview01'>1qqp</scene>, resolution 1.90Å | |PDB= 1qqp |SIZE=350|CAPTION= <scene name='initialview01'>1qqp</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=IDU:1,4-DIDEOXY-O2-SULFO-GLUCURONIC+ACID'>IDU</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqp OCA], [http://www.ebi.ac.uk/pdbsum/1qqp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qqp RCSB]</span> | |||
}} | }} | ||
| Line 38: | Line 41: | ||
[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:37 2008'' | ||
Revision as of 20:17, 30 March 2008
| |||||||||||||
| 1qqp, resolution 1.90Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | IDU, SGN | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 Sun Mar 30 23:17:37 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
