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Solution Structure of the Coxsackievirus and Adenovirus Receptor Domain 1,

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journal contribution
posted on 24.02.2004, 00:00 by Shaokai Jiang, Amy Jacobs, Thomas M. Laue, Michael Caffrey
The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer−dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure.

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