Research Activities
Our goal is to understand the molecular mechanism of synaptic neurotransmission. We are interested in the structure, function, and dynamics of key players in the synaptic vesicle fusion machinery. Our lab is also working on the mechanism of action of clostridial neurotoxins that target this machinery. Other projects include protein complexes that are involved in synaptic development and the ATPases of the AAA family that are involved in protein complex disassembly and degradation. A molecular understanding of these complex protein machineries may ultimately lead to new therapeutics to treat human diseases.
Selected Projects Recent Publications

schematic diagram of how synaptic vesicle fusion occurs assisted by SNAREs

Synaptic Vesicle Fusion

Diagram of BoNTA light chain on the surface of a cell

Mechanism of Clostridial Neurotoxins

  J.Ko, C. Zhang, D. Arac, A.A. Boucard, A.T. Brunger, T.C. Sudhof, Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation. Embo J.28, 3244-3255 (2009)

 A.T.Brunger, A.Rummel, Receptor and substrate interactions of clostridial neurotoxins. Toxicon 54, 550-560 (2009).

 M.J.Schnieders,T.D.Fenn,V.S.Pande, A.T.Brunger, Polarizable atomic multipole X-ray refinement: application to peptide crystals. Acta Cryst. D65, 952-965 (2009).

 A.T. Brunger, K. Weninger, M. Bowen, S Chu, Single-molecule studies of the neuronal SNARE fusion machinery. Ann. Rev. Biochem.78, 903-928 (2009).

 W. Li, D. Tu, L. Li, R. Ghirlando, A.T. Brunger, Y. Ye, Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2ge. Proc. Natl. Acad. Sci. USA 106, 3722-3727 (2009).

 A.T. Brunger, B. DeLaBarre, J.M. Davies, and W.I. Weis. X-ray structure determination at low resolution. Acta Cryst D56, 128-133 (2009).

 J.E. Zuniga, J.J. Schmidt, T. Fenn, J.C. Burnett, D, Arac, R. Gussio, R.G. Stafford, S,S. Badie, S. Bavari, and A.T. Brunger, A potent peptidomimetic inhibitor of botulinum neurotoxin serotype A has a very different conformation than SNAP-25 substrate. Structure 16, 1588-1597 (2008).

View all projects View all publications