1HRI

STRUCTURE DETERMINATION OF ANTIVIRAL COMPOUND SCH 38057 COMPLEXED WITH HUMAN RHINOVIRUS 14

Summary for 1HRI

• Entry DOI: 10.2210/pdb1hri/pdb
• Descriptor: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1), HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2), HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3), ... (5 entities in total)
• Functional Keywords: coat protein, icosahedral virus, virus
• Biological source: Human rhinovirus 14; 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): P03303 P03303 P03303 P03303
• Total number of polymer chains: 4
• Total formula weight: 94791.33

Authors

Zhang, A.,Nanni, R.G.,Oren, D.A.,Arnold, E. (deposition date: 1992-10-01, release date: 1993-10-31, Last modification date: 2024-05-22)

Primary citation

Zhang, A.,Nanni, R.G.,Li, T.,Arnold, G.F.,Oren, D.A.,Jacobo-Molina, A.,Williams, R.L.,Kamer, G.,Rubenstein, D.A.,Li, Y.,Rozhon, E.,Cox, S.,Buontempo, P.,O'Connell, J.,Schwartz, J.,Miller, G.,Bauer, B.,Versace, R.,Pinto, P.,Ganguly, A.,Girijavallabhan, V.,Arnold, E.
Structure determination of antiviral compound SCH 38057 complexed with human rhinovirus 14.
J.Mol.Biol., 230:857-867, 1993

PubMed Abstract: SCH 38057 (1-[6-(2-chloro-4-methoxyphenoxy)-hexyl]imidazole hydrochloride) is a new, water-soluble antiviral compound that has inhibitory activities against a number of picornavirus infections. The structure of the human rhinovirus 14 (HRV14) complex with SCH 38057 was determined at 3.0 A resolution by single-crystal diffraction techniques using synchrotron X-radiation. SCH 38057 was found to bind at the innermost end of the hydrophobic pocket within the capsid protein VP1, a locus of binding of other antipicornaviral agents; however, the complex differs from previously reported complexes in two important aspects. It leaves a considerable volume near the entrance to the binding pocket unoccupied. In addition, the alterations in the conformation of the VP1 polypeptide are similar to, but more extensive than those observed in HRV14 complexes with other antiviral agents. Although only 9 amino acids of VP1 have close contacts with the SCH 38057 molecule (within 3.6 A), at least 36 amino acids from both VP1 and VP3 have significantly altered conformations (C alpha movement > 0.5 A versus native). The structures of complexes of HRV14 with SCH 38057 and WIN 51711 are compared. Aromatic ring interactions between picornavirus capsid residues and antiviral inhibitors are proposed to be among the major determinants for positioning of these compounds.

PubMed: 8386772
DOI: 10.1006/jmbi.1993.1206

Experimental method

X-RAY DIFFRACTION (3 Å)