Title | The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view. | ||
Author | Hewat, E A; Neumann, E; Conway, J F; Moser, R; Ronacher, B; Marlovits, T C; Blaas, D | ||
Journal | EMBO J | Publication Year/Month | 2000-Dec |
PMID | 11101504 | PMCID | PMC305862 |
Affiliation | 1.Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble, France. |
Human rhinovirus serotype 2 (HRV2) belongs to the minor group of HRVs that bind to members of the LDL-receptor family including the very low density lipoprotein (VLDL)-receptor (VLDL-R). We have determined the structures of the complex between HRV2 and soluble fragments of the VLDL-R to 15 A resolution by cryo-electron microscopy. The receptor fragments, which include the first three ligand-binding repeats of the VLDL-R (V1-3), bind to the small star-shaped dome on the icosahedral 5-fold axis. This is in sharp contrast to the major group of HRVs where the receptor site for ICAM-1 is located at the base of a depression around each 5-fold axis. Homology models of the three domains of V1-3 were used to explore the virus-receptor interaction. The footprint of VLDL-R on the viral surface covers the BC- and HI-loops on VP1.