Abstract
The Coxsackie virus and Adenovirus Receptor (CAR) plays a dual role as a viral receptor and a homotypic junctional adhesion protein. CAR is a transmembrane protein and a member of the Immunoglobulin superfamily with two extracellular Ig-like domains. According to x-ray crystallographic data, the most distal Ig-like domain (D1) mediates the homophilic interaction. This same domain is also responsible for the high affinity binding of the adenovirus (Ad) fiber protein. Currently no activity has been ascribed to the proximal Ig-like domain (D2). We asked whether the D2 domain plays a role in the function of CAR as either a viral receptor or an adhesion protein.
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