Solution structure of the coxsackievirus and adenovirus receptor domain 1
Abstract
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.
Department
Molecular, Cellular and Biomedical Sciences
Publication Date
1-30-2004
Journal Title
Biochemistry
Publisher
ACS Publications
Digital Object Identifier (DOI)
Document Type
Article
Recommended Citation
Jiang S, Jacobs A, Laue TM, Caffrey M. (2004) "Solution structure of the coxsackievirus and adenovirus receptor domain 1." Biochemistry, 43, 1847-53.