Journal
BIOCHEMISTRY
Volume 49, Issue 8, Pages 1776-1786Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi901942m
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Biochemical Studies have determined that reoviruses attach to cells by combining attachment protein sigma 1 to the binding interface of its receptor protein junctional adhesion molecule A (JAM-A), and the interface normally takes care of the homodimerization of JAM-A. Tighter binding and slower dissociation of for the sigma 1-JAM complex than for the JAM-JAM complex have been probed by both biological and atomic force microscopy experiments; however, the mechanism of the binding preference of the attachment protein for JAM-A still remains unclear. With the help of classical and steered molecular dynamics and energy calculations, the unbinding forces and kinetic properties of the complexes are investigated, together with detailed structural information analyses. A multireceptor mechanism is proposed for the binding preference, which can be helpful for future viral Infection and vector targeting studies.
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