1R1A

CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS SEROTYPE 1A (HRV1A)

Summary for 1R1A

• Entry DOI: 10.2210/pdb1r1a/pdb
• Related PRD ID: PRD_900003
• Descriptor: HUMAN RHINOVIRUS 1A COAT PROTEIN (SUBUNIT VP1), HUMAN RHINOVIRUS 1A COAT PROTEIN (SUBUNIT VP2), HUMAN RHINOVIRUS 1A COAT PROTEIN (SUBUNIT VP3), ... (5 entities in total)
• Functional Keywords: rhinovirus coat protein, icosahedral virus, virus
• Biological source: Human rhinovirus 1A; More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion: P23008 P23008 P23008 P23008
• Total number of polymer chains: 4
• Total formula weight: 92828.56

Authors

Kim, S.,Rossmann, M.G. (deposition date: 1989-03-15, release date: 1990-07-15, Last modification date: 2024-12-25)

Primary citation

Kim, S.S.,Smith, T.J.,Chapman, M.S.,Rossmann, M.G.,Pevear, D.C.,Dutko, F.J.,Felock, P.J.,Diana, G.D.,McKinlay, M.A.
Crystal structure of human rhinovirus serotype 1A (HRV1A).
J.Mol.Biol., 210:91-111, 1989

PubMed Abstract: The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 A resolution using phase refinement and extension by symmetry averaging starting with phases at 5 A resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.

PubMed: 2555523
DOI: 10.1016/0022-2836(89)90293-3

Experimental method

X-RAY DIFFRACTION (3.2 Å)