1xr7: Difference between revisions

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New page: left|200px<br /><applet load="1xr7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xr7, resolution 2.30Å" /> '''Crystal structure of...
 
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[[Image:1xr7.gif|left|200px]]<br /><applet load="1xr7" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1xr7.gif|left|200px]]<br /><applet load="1xr7" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1xr7, resolution 2.30&Aring;" />
caption="1xr7, resolution 2.30&Aring;" />
'''Crystal structure of RNA-dependent RNA Polymerase 3D from human rhinovirus serotype 16'''<br />
'''Crystal structure of RNA-dependent RNA Polymerase 3D from human rhinovirus serotype 16'''<br />


==Overview==
==Overview==
Human rhinoviruses (HRV), the predominant members of the Picornaviridae, family of positive-strand RNA viruses, are the major causative agents of, the common cold. Given the lack of effective treatments for rhinoviral, infections, virally encoded proteins have become attractive therapeutic, targets. The HRV genome encodes an RNA-dependent RNA polymerase (RdRp), denoted 3Dpol, which is responsible for replicating the viral genome and, for synthesizing a protein primer used in the replication. Here the, crystal structures for three viral serotypes (1B, 14, and 16) of HRV 3Dpol, have been determined. The three structures are very similar to one, another, and to the closely related poliovirus (PV) 3Dpol enzyme. Because, the reported PV crystal structure shows significant disorder, HRV 3Dpol, provides the first complete view of a picornaviral RdRp. The folding, topology of HRV 3Dpol also resembles that of RdRps from hepatitis C virus, (HCV) and rabbit hemorrhagic disease virus (RHDV) despite very low, sequence homology.
Human rhinoviruses (HRV), the predominant members of the Picornaviridae family of positive-strand RNA viruses, are the major causative agents of the common cold. Given the lack of effective treatments for rhinoviral infections, virally encoded proteins have become attractive therapeutic targets. The HRV genome encodes an RNA-dependent RNA polymerase (RdRp) denoted 3Dpol, which is responsible for replicating the viral genome and for synthesizing a protein primer used in the replication. Here the crystal structures for three viral serotypes (1B, 14, and 16) of HRV 3Dpol have been determined. The three structures are very similar to one another, and to the closely related poliovirus (PV) 3Dpol enzyme. Because the reported PV crystal structure shows significant disorder, HRV 3Dpol provides the first complete view of a picornaviral RdRp. The folding topology of HRV 3Dpol also resembles that of RdRps from hepatitis C virus (HCV) and rabbit hemorrhagic disease virus (RHDV) despite very low sequence homology.


==About this Structure==
==About this Structure==
1XR7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2]. This structure superseeds the now removed PDB entry 1TE9. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XR7 OCA].  
1XR7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2]. This structure supersedes the now removed PDB entry 1TE9. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XR7 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Diehl, W.]]
[[Category: Diehl, W.]]
[[Category: Dragovich, P.S.]]
[[Category: Dragovich, P S.]]
[[Category: Ferre, R.A.]]
[[Category: Ferre, R A.]]
[[Category: Fuhrman, S.A.]]
[[Category: Fuhrman, S A.]]
[[Category: Lingardo, L.K.]]
[[Category: Lingardo, L K.]]
[[Category: Love, R.A.]]
[[Category: Love, R A.]]
[[Category: Maegley, K.A.]]
[[Category: Maegley, K A.]]
[[Category: Parge, H.E.]]
[[Category: Parge, H E.]]
[[Category: Yu, X.]]
[[Category: Yu, X.]]
[[Category: rna-dependent rna polymerase]]
[[Category: rna-dependent rna polymerase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:16:58 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:46 2008''

Revision as of 16:57, 21 February 2008

File:1xr7.gif


1xr7, resolution 2.30Å

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Crystal structure of RNA-dependent RNA Polymerase 3D from human rhinovirus serotype 16

OverviewOverview

Human rhinoviruses (HRV), the predominant members of the Picornaviridae family of positive-strand RNA viruses, are the major causative agents of the common cold. Given the lack of effective treatments for rhinoviral infections, virally encoded proteins have become attractive therapeutic targets. The HRV genome encodes an RNA-dependent RNA polymerase (RdRp) denoted 3Dpol, which is responsible for replicating the viral genome and for synthesizing a protein primer used in the replication. Here the crystal structures for three viral serotypes (1B, 14, and 16) of HRV 3Dpol have been determined. The three structures are very similar to one another, and to the closely related poliovirus (PV) 3Dpol enzyme. Because the reported PV crystal structure shows significant disorder, HRV 3Dpol provides the first complete view of a picornaviral RdRp. The folding topology of HRV 3Dpol also resembles that of RdRps from hepatitis C virus (HCV) and rabbit hemorrhagic disease virus (RHDV) despite very low sequence homology.

About this StructureAbout this Structure

1XR7 is a Single protein structure of sequence from Human rhinovirus 2. This structure supersedes the now removed PDB entry 1TE9. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy., Love RA, Maegley KA, Yu X, Ferre RA, Lingardo LK, Diehl W, Parge HE, Dragovich PS, Fuhrman SA, Structure. 2004 Aug;12(8):1533-44. PMID:15296746

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