1XR5

Crystal Structure of the RNA-dependent RNA Polymerase 3D from human rhinovirus serotype 14

Replaces:  1TEB

Summary for 1XR5

• Entry DOI: 10.2210/pdb1xr5/pdb
• Related: 1TE8 1TE9 1TEB 1XR6 1XR7
• Descriptor: Genome polyprotein, SAMARIUM (III) ION (3 entities in total)
• Functional Keywords: rna-dependent rna polymerase, transferase
• Biological source: Human rhinovirus 14
• Cellular location: Protein 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): P03303
• Total number of polymer chains: 1
• Total formula weight: 53289.26

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 citation

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.
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

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)