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Schematic representation of the protein constructs used in this study.

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posted on 31.10.2017 by Michelle P. Christie, Shu-Hong Hu, Andrew E. Whitten, Asma Rehman, Russell J. Jarrott, Gordon J. King, Brett M. Collins, Jennifer L. Martin

In vivo full-length Sx consists of an N-peptide preceding an N-terminal α-helical bundle (the Habc domain), a SNARE motif (the H3 helix) and a C-terminal transmembrane region. We used soluble Sx1 and Sx4 constructs lacking the transmembrane domain for experiments reported here. ΔN indicates Sx constructs lacking the N-peptide. Munc18 and SNAP25 and VAMP2 constructs used in these experiments are also shown. The positions of engineered fusion tags and protease cleavage sites are as indicated.

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