1po2: Difference between revisions

Revision as of 15:30, 21 February 2008

POLIOVIRUS (TYPE 1, MAHONEY) IN COMPLEX WITH R77975, AN INHIBITOR OF VIRAL REPLICATION

OverviewOverview

Crystal structures of the Mahoney strain of type 1 poliovirus complexed with the antiviral compounds R80633 and R77975 were determined at 2.9 A resolution. These compounds block infection by preventing conformational changes required for viral uncoating. In various drug-poliovirus complexes reported earlier, no significant conformational changes were found in the structures of the capsid proteins. In the structures reported here, the strain of virus is relatively insensitive to these antivirals. Correspondingly, significant conformational changes are necessary to accommodate the drug. These conformational changes affect both the immediate vicinity of the drug binding site, and more distant loops located near the fivefold axis. In addition, small but concerted shifts of the centers of mass of the major capsid proteins consistently have been detected whose magnitudes are correlated inversely with the effectiveness of the drugs. Collectively, the drug complexes appear to sample the conformational repertoire of poliovirus near equilibrium, and thus provide a possible model for the earliest stages of viral uncoating during infection.

About this StructureAbout this Structure

1PO2 is a Protein complex structure of sequences from Human poliovirus 1 with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Ligand-induced conformational changes in poliovirus-antiviral drug complexes., Hiremath CN, Filman DJ, Grant RA, Hogle JM, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):558-70. PMID:15299887

Page seeded by OCA on Thu Feb 21 14:30:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1po2.gif|left|200px]]<br /><applet load="1po2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1po2.gif|left|200px]]<br /><applet load="1po2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1po2, resolution 2.9&Aring;" />
 '''POLIOVIRUS (TYPE 1, MAHONEY) IN COMPLEX WITH R77975, AN INHIBITOR OF VIRAL REPLICATION'''<br />
 ==Overview==
-Crystal structures of the Mahoney strain of type 1 poliovirus complexed, with the antiviral compounds R80633 and R77975 were determined at 2.9 A, resolution. These compounds block infection by preventing conformational, changes required for viral uncoating. In various drug-poliovirus complexes, reported earlier, no significant conformational changes were found in the, structures of the capsid proteins. In the structures reported here, the, strain of virus is relatively insensitive to these antivirals., Correspondingly, significant conformational changes are necessary to, accommodate the drug. These conformational changes affect both the, immediate vicinity of the drug binding site, and more distant loops, located near the fivefold axis. In addition, small but concerted shifts of, the centers of mass of the major capsid proteins consistently have been, detected whose magnitudes are correlated inversely with the effectiveness, of the drugs. Collectively, the drug complexes appear to sample the, conformational repertoire of poliovirus near equilibrium, and thus provide, a possible model for the earliest stages of viral uncoating during, infection.
+Crystal structures of the Mahoney strain of type 1 poliovirus complexed with the antiviral compounds R80633 and R77975 were determined at 2.9 A resolution. These compounds block infection by preventing conformational changes required for viral uncoating. In various drug-poliovirus complexes reported earlier, no significant conformational changes were found in the structures of the capsid proteins. In the structures reported here, the strain of virus is relatively insensitive to these antivirals. Correspondingly, significant conformational changes are necessary to accommodate the drug. These conformational changes affect both the immediate vicinity of the drug binding site, and more distant loops located near the fivefold axis. In addition, small but concerted shifts of the centers of mass of the major capsid proteins consistently have been detected whose magnitudes are correlated inversely with the effectiveness of the drugs. Collectively, the drug complexes appear to sample the conformational repertoire of poliovirus near equilibrium, and thus provide a possible model for the earliest stages of viral uncoating during infection.
 ==About this Structure==
-PO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1] with MYR and J77 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PO2 OCA].
+PO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=J77:'>J77</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PO2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Human poliovirus 1]]
 [[Category: Protein complex]]
-[[Category: Filman, D.J.]]
+[[Category: Filman, D J.]]
-[[Category: Grant, R.A.]]
+[[Category: Grant, R A.]]
-[[Category: Hiremath, C.N.]]
+[[Category: Hiremath, C N.]]
-[[Category: Hogle, J.M.]]
+[[Category: Hogle, J M.]]
 [[Category: J77]]
 [[Category: MYR]]
@@ Line 26: / Line 26: @@
 [[Category: thiol protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:57:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:42 2008''