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1R09

HUMAN RHINOVIRUS 14 COMPLEXED WITH ANTIVIRAL COMPOUND R 61837

Summary for 1R09
Entry DOI10.2210/pdb1r09/pdb
Related1R08 2R04 2R06 2R07 2RM2 2RR1 2RS1 2RS3 2RS5
DescriptorHUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1), HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2), HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3), ... (7 entities in total)
Functional Keywordsrhinovirus coat protein, icosahedral virus, virus
Biological sourceHuman rhinovirus 14
More
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): P03303 P03303 P03303 P03303
Total number of polymer chains4
Total formula weight94845.02
Authors
Chapman, M.S.,Minor, I.,Rossmann, M.G.,Diana, G.D.,Andries, K. (deposition date: 1990-05-04, release date: 1991-10-15, Last modification date: 2024-05-22)
Primary citationChapman, M.S.,Minor, I.,Rossmann, M.G.,Diana, G.D.,Andries, K.
Human rhinovirus 14 complexed with antiviral compound R 61837.
J.Mol.Biol., 217:455-463, 1991
Cited by
PubMed Abstract: The binding of the antirhinoviral agent R 61837 to human rhinovirus 14 has been examined by X-ray crystallographic methods. The compound R 61837 binds in the same pocket (underneath the canyon floor) as the "WIN" antirhinoviral agents. It does not penetrate as far into the pocket but causes similar conformational changes in the virus capsid. The movement of residues 1217 to 1221 of viral protein 1 (in the "FMDV loop") is more pronounced for R 61837 than for WIN compounds. Although both R 61837 and WIN antiviral agents partially fill the same hydrophobic pocket, atomic binding interactions differ, showing that considerable diversity in the nature of antiviral agents is possible.
PubMed: 1847215
DOI: 10.1016/0022-2836(91)90749-V
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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