Journal
PROTEIN SCIENCE
Volume 16, Issue 3, Pages 539-542Publisher
WILEY
DOI: 10.1110/ps.062643507
Keywords
adenovirus; CAR; cell adhesion; coxsackievirus; NMR
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Funding
- NCRR NIH HHS [S10 RR15757] Funding Source: Medline
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The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus and adenovirus. CAR possesses an extracellular region that is comprised of 2 immunoglobulin domains termed CAR-D1 and CAR-D2. In the present work, the solution structure of CAR-D2, consisting of residues 142-235 of human CAR, has been determined by NMR spectroscopy. CAR-D2 is shown to be a beta-sandwich motif comprised of two beta-sheets, which are stabilized by two disulfide bonds. The first beta-sheet is comprised of beta-strands A, B, and E, and the second b-sheet is comprised of beta-strands C, F, and G. A relatively hydrophobic helix is found between beta-strands C and E, which replaces beta-strand D of the classical c-type immunoglobulin fold.
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