Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR. Journal   Science. Citation   Science. 286(5444):1579-83 Publication date   1999 Nov 19 Authors   Bewley MC Springer K Zhang YB Freimuth P Flanagan JM Investigators   Maria C. Bewley John M. Flanagan Grant agencies   National Center for Research Resources Grants   NCRR 1P41 RR12408-01A1 MeSH headings   Adenoviruses, Human Capsid Capsid Proteins Receptors, Virus MeSH qualifiers   metabolism chemistry Abstract   Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors. Medline ID   20036898