Rachelle Gaudet
Structural biology of membrane transport

X-ray crystallography and other biophysical and biochemical techniques are combined to study the stereochemistry of signaling and transport through biological membranes. Studies focus on two subjects. First, a diverse family of TRP channels, with particular emphasis on how certain members of this group sense and respond to heat and pain. Second, TAP, the transporter associated with antigen processing, which moves peptides generated by the proteosome in the cytosol into the endoplasmic reticulum.

Publications:
Misaghi, S., Galardy, P.J., Meester, W.J., Ovaa, H., Ploegh, H.L. and Gaudet, R. 2005. Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J. Biol. Chem. 280: 1512-1520.

Gaudet, R. and Wiley, D.C. 2001. Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J. 20: 4964-4972.

Gaudet, R., Bohm, A. and Sigler, P.B. 1996. Crystal structure at 2.4A resolution of the complex of transducin bg and its regulator, phosducin. Cell 87: 577-588.