1FPN
HUMAN RHINOVIRUS SEROTYPE 2 (HRV2)
Summary for 1FPN
| Entry DOI | 10.2210/pdb1fpn/pdb |
| Descriptor | COAT PROTEIN VP1, COAT PROTEIN VP2, COAT PROTEIN VP3, ... (6 entities in total) |
| Functional Keywords | human rhinovirus, pocket factor, rhinovirus coat protein, icosahedral virus, virus |
| Biological source | Human rhinovirus 2 More |
| 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): P04936 P04936 P04936 P04936 |
| Total number of polymer chains | 4 |
| Total formula weight | 95599.47 |
| Authors | Verdaguer, N.,Blaas, D.,Fita, I. (deposition date: 2000-08-31, release date: 2000-09-20, Last modification date: 2024-02-07) |
| Primary citation | Verdaguer, N.,Blaas, D.,Fita, I. Structure of human rhinovirus serotype 2 (HRV2). J.Mol.Biol., 300:1179-1194, 2000 Cited by PubMed Abstract: Human rhinoviruses are classified into a major and a minor group based on their binding to ICAM-1 or to members of the LDL-receptor family, respectively. They can also be divided into groups A and B, according to their sensitivity towards a panel of antiviral compounds. The structure of human rhinovirus 2 (HRV2), which uses the LDL receptor for cell attachment and is included in antiviral group B, has been solved and refined at 2.6 A resolution by X-ray crystallography to gain information on the peculiarities of rhinoviruses, in particular from the minor receptor group. The main structural differences between HRV2 and other rhinoviruses, including the minor receptor group serotype HRV1A, are located at the internal protein shell surface and at the external antigenic sites. In the interior, the N termini of VP1 and VP4 form a three-stranded beta-sheet in an arrangement similar to that present in poliovirus, although myristate was not visible at the amino terminus of VP4 in the HRV2 structure. The betaE-betaF loop of VP2, a linear epitope within antigenic site B recognized by monoclonal antibody 8F5, adopts a conformation considerably different from that found in the complex of 8F5 with a synthetic peptide of the same sequence. This either points to considerable structural changes impinged on this loop upon antibody binding, or to the existence of more than one single conformation of the loop when the virus is in solution. The hydrophobic pocket of VP1 was found to be occupied by a pocket factor apparently identical with that present in the major receptor group virus HRV16. Electron density, consistent with the presence of a viral RNA fragment, is seen stacked against a conserved tryptophan residue. PubMed: 10903863DOI: 10.1006/jmbi.2000.3943 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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