1qqp: Difference between revisions

Revision as of 15:42, 21 February 2008

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

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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OCA

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-[[Image:1qqp.gif|left|200px]]<br /><applet load="1qqp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qqp.gif|left|200px]]<br /><applet load="1qqp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qqp, resolution 1.90&Aring;" />
 '''FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.'''<br />
 ==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.
+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==
-QQP 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 superseeds the now removed PDB entry 1FHP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QQP OCA].
+QQP 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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Abu-Ghazaleh, R.]]
-[[Category: Blakemore, W.E.]]
+[[Category: Blakemore, W E.]]
-[[Category: Ellard, F.M.]]
+[[Category: Ellard, F M.]]
-[[Category: Fry, E.E.]]
+[[Category: Fry, E E.]]
 [[Category: Jackson, T.]]
-[[Category: King, A.M.Q.]]
+[[Category: King, A M.Q.]]
-[[Category: Lea, S.M.]]
+[[Category: Lea, S M.]]
-[[Category: Newman, J.W.I.]]
+[[Category: Newman, J W.I.]]
 [[Category: Samuel, A.]]
-[[Category: Stuart, D.I.]]
+[[Category: Stuart, D I.]]
 [[Category: heparan sulphate]]
 [[Category: icosahedral virus]]
@@ Line 29: / Line 29: @@
 [[Category: virus/viral protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:20:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:40 2008''