(A) Ribbon diagram of the mammalian complexin-SNARE crystal structure (Chen et al., 2002) using PDB code 1KIL. Cytoplasmic SNARE domains from synaptobrevin (red), Syntaxin (yellow), and SNAP-25 (gree…
Alignments of the alpha helical regions of complexin across 16 species from seven phyla using Clustal Omega multiple sequence alignment. The accessory helix region (orange) was defined based on …
(A) Agadir helicity predictions for human (Hs, blue), ctenophore (Ml, pink), placazoa (Ta, green), and worm (Ce, dashed line) complexin homologs, plotted relative to the first residue of the central …
(A) Two deletions within the worm AH domain were used: ΔAHshort (35–49, red) and ΔAHlong (30–50, aqua). (B) Examples of spontaneous EPSCs in zero external Ca2+ for wild-type, cpx-1, and transgenic …
(A) Schematic of a worm depicting the region imaged for axonal expression (pink box). All rescuing transgenes were quantified by imaging the C-terminal GFP tag in single axons of immobilized intact …
(A) Two chimeric CPX-1 constructs substituting worm AH with the mouse AH. The long form (mouse AH) substitutes worm residues 26–49 with mouse residues 24–47 whereas the short form (mouse AHshort) …
(A) The AH hydrophobic moment was computed with angular orientation relative to the first residue of the CH. (B) Example of a hydrophobic moment for a particular AH (worm). (C) Polar plot of the …
The helical region of the AH domain was defined using Agadir with a criterion of >5% predicted helicity for a continuous region N-terminal to the CH domain. The net formal charge within this stretch …
(A) NMR derived Cα-Cβ shifts from either wild-type (black) or R43P (blue) worm CPX-1 peptide missing the C-terminal domain. R43P is indicated in red. Below, the predicted helical content using …
(A) AH and CH helical content based on Agadir predictions is plotted for wild-type CPX-1 and three variants with a single substitution at residue 43 as indicated. (B) Average helical content of the …
(A) Schematic of the helix substitution strategy. A(EAAK)7A sequences were substituted for residues 26–49 in the worm AH domain. (B) Agadir prediction for helical stability of the 7-turn helix motif …
Charge density of the AH domain in seven rescuing CPX-1 variants. Green indicates nearly complete rescue, gray is partial, and red is poor rescue as measured by aldicarb sensitivity. The CPX-1 …
Polar plot of hydrophobic moments for the AH domain of CPX-1 variants. The CPX-1 variants (blue) are mouse AHshort (SM), worm AH with hydrophobic to glutamates (w[h→E]), mouse AH with hydrophobic to …