TY - CHAP
T1 - The coxsackievirus and adenovirus receptor
AU - Freimuth, P.
AU - Philipson, L.
AU - Carson, S. D.
PY - 2008
Y1 - 2008
N2 - The coxsackievirus and adenovirus receptor (CAR) has been studied extensively since its identification and isolation in 1997. The CAR is an immunoglobulin superfamily protein with two extracellular Ig-like domains, a single membrane-spanning sequence, and a significant cytoplasmic domain. It is structurally and functionally similar to the junctional adhesion molecules. The amino terminal domain, distal from the membrane, has been structurally characterized alone, bound to the adenovirus fiber knob, and, in full-length CAR, docked in the canyon structure of the coxsackievirus capsid. Although the past decade has produced a burst of new knowledge about CAR, significant questions concerning its function in normal physiology and coxsackievirus- related pathology remain unanswered.
AB - The coxsackievirus and adenovirus receptor (CAR) has been studied extensively since its identification and isolation in 1997. The CAR is an immunoglobulin superfamily protein with two extracellular Ig-like domains, a single membrane-spanning sequence, and a significant cytoplasmic domain. It is structurally and functionally similar to the junctional adhesion molecules. The amino terminal domain, distal from the membrane, has been structurally characterized alone, bound to the adenovirus fiber knob, and, in full-length CAR, docked in the canyon structure of the coxsackievirus capsid. Although the past decade has produced a burst of new knowledge about CAR, significant questions concerning its function in normal physiology and coxsackievirus- related pathology remain unanswered.
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U2 - 10.1007/978-3-540-75546-3_4
DO - 10.1007/978-3-540-75546-3_4
M3 - Chapter
C2 - 18357766
AN - SCOPUS:43649097432
SN - 9783540755456
T3 - Current Topics in Microbiology and Immunology
SP - 67
EP - 87
BT - Group B Coxsackieviruses
PB - Springer Verlag
ER -