Fusion allows the virus genome into the host cell where it replicates. The protein conformational change and its interaction with the cellular membranes are, however, largely unknown. In our laboratory we express the membrane interacting domain of HA in E. coli. Spin labeling EPR and the crystallographic studies are pursued in parallel to elucidate the mechanism of HA-mediated membrane fusion. Thus, the effort also involves the understanding of the function of HIV gp160.
Every living cell possesses the ability to respond to external signals.
Specific receptor proteins in cell membranes recognize light, nutrients, odorants, hormones, and neurotransmitters in order to initiate specific physiological responses in cells. It is remarkable that many functional receptors share the basic structural organization. Thus, each class of receptors might as well have a common signalling mechanism. The primary step in signal transduction is the dynamic response of the receptor which converts a chemical stimulus to a structural message and then transduce it across the membrane through a proper conformational change. Our objective is to define and characterize motion of structural units in the receptor that constitutes transmembrane signal transmission.