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1XR7

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

Replaces:  1TE9
Summary for 1XR7
Entry DOI10.2210/pdb1xr7/pdb
Related1TE8 1TE9 1TEB 1XR5 1XR6
DescriptorGenome polyprotein (2 entities in total)
Functional Keywordsrna-dependent rna polymerase, transferase
Biological sourceHuman rhinovirus 16
Cellular locationProtein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): Q82122
Total number of polymer chains2
Total formula weight104572.00
Authors
Love, R.A.,Maegley, K.A.,Yu, X.,Ferre, R.A.,Lingardo, L.K.,Diehl, W.,Parge, H.E.,Dragovich, P.S.,Fuhrman, S.A. (deposition date: 2004-10-13, release date: 2004-10-26, Last modification date: 2024-02-14)
Primary citationLove, R.A.,Maegley, K.A.,Yu, X.,Ferre, R.A.,Lingardo, L.K.,Diehl, W.,Parge, H.E.,Dragovich, P.S.,Fuhrman, S.A.
The Crystal Structure of the RNA-Dependent RNA Polymerase from Human Rhinovirus: A Dual-Function Target for Common Cold Antiviral Therapy
Structure, 12:1533-1544, 2004
Cited by
PubMed Abstract: 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.
PubMed: 15296746
DOI: 10.1016/j.str.2004.05.024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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