Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide
Michelle P Christie, Andrew E Whitten, Gordon J King, Shu-Hong Hu, Russell J Jarrott, Kai-En Chen, Anthony P Duff, Philip Callow, Brett M Collins, David E James, Jennifer L Martin
Proceedings of the National Academy of Sciences | NATL ACAD SCIENCES | Published : 2012
Awarded by National Health and Medical Research Council (NHMRC)
Awarded by Australian Government
We thank Jill Trewhella, Kevin Jack, and Nathan Cowieson for help with SAXS and Alun Jones for mass spectrometric measurements. This work was supported by National Health and Medical Research Council (NHMRC) Program 535921. A.E.W. is an NHMRC Peter Doherty Fellow (569864); B.M.C. is an Australian Research Council (ARC) Future Fellow (FT100100027), D.E.J. is an NHMRC Senior Principal Research Fellow (1019680), and J.L.M. is an ARC Australian Laureate Fellow (FL0992138) and honorary NHMRC Fellow (455829). Protein deuteration at the National Deuteration Facility was partly funded by the National Collaborative Research Infrastructure Strategy of the Australian Government. Recombinant expression of Munc18c was performed at the University of Queensland Protein Expression Facility. We also acknowledge financial support from the Access to Major Research Facilities Program of the Australian Government (08/09-N-47) and access to the SAXS/WAXS beamline at the Australian Synchrotron.