Volume 4, Issue 4, Pages (April 1996)

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Volume 4, Issue 4, Pages 417-423 (April 1996) The 1.1 å crystal structure of the neuronal acetylcholine receptor antagonist, α- conotoxin PnIA from Conus pennaceus Shu-Hong Hu, John Gehrmann, Luke W Guddat, Paul F Alewood, David J Craik, Jennifer L Martin Structure Volume 4, Issue 4, Pages 417-423 (April 1996) DOI: 10.1016/S0969-2126(96)00047-0

Figure 1 Conotoxin frameworks. (a) The structural frameworks of the four major classes of conotoxins, with their distinctive disulfide bond pattern indicated. (b) Sequence alignment of α-conotoxins from various Conidae with cysteine residues highlighted: PnIA and PnIB from C. pennaceus [8]; GI, GIA and GII from C. geographus [3]; MI from C. magus [33]; SI, SIA and SII from C. striatus [9]; ImI from C. imperialis [10]; and EI from C. ermineus [11]. The letter O in the sequence of EI represents hydroxyproline. Asterisks indicate an amidated C terminus. Hyphens indicate gaps in the sequence alignment. Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 2 2Fo−Fc electron-density map. The quality and resolution of the final 2Fo−Fc electron-density map is shown in the region of the structure corresponding to Tyr15 and the disulfide bond formed between Cys3 and Cys16. Electron density is contoured at 1σ. Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 3 Structure of PnIA. (a) The backbone fold of PnIA (green) and the two disulfide bonds (yellow) are shown. The surface of the molecule is in blue and the N and C termini are labeled. (b) Space-filling model of PnIA. The positively charged N-terminal amine is in blue, cysteine side chains (Cys2, Cys3, Cys8 and Cys16) in yellow, polar side chains (Ser4, Asn11 and Asn12) in cyan, Tyr15 side chain in magenta and the negatively charged Asp14 side chain in red. Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 3 Structure of PnIA. (a) The backbone fold of PnIA (green) and the two disulfide bonds (yellow) are shown. The surface of the molecule is in blue and the N and C termini are labeled. (b) Space-filling model of PnIA. The positively charged N-terminal amine is in blue, cysteine side chains (Cys2, Cys3, Cys8 and Cys16) in yellow, polar side chains (Ser4, Asn11 and Asn12) in cyan, Tyr15 side chain in magenta and the negatively charged Asp14 side chain in red. Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 4 Stereo plot of the PnIA structure. Cysteine and charged residues are labelled and intramolecular hydrogen bonds are indicated by dashed lines (3.3 å cutoff). Oxygen atoms are in red, sulfurs in yellow and nitrogen atoms are in blue. Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 5 Surface representation of PnIA. Four views of the molecular surface of PnIA, coloured according to electrostatic potential (blue for positive, red for negative, white for hydrophobic and pale blue/red for polar regions). Charges were taken from XPLOR tophcsdx.pro [28]. The views are 90° incremental rotations around the vertical axis. (a) Surface of PnIA, shown in the same orientation as Figure 3. (b) View rotated 90° around the vertical axis. (c) View rotated 180° around the vertical axis. (d) View rotated 270° around the vertical axis. (Figures were generated using GRASP [34].) Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 5 Surface representation of PnIA. Four views of the molecular surface of PnIA, coloured according to electrostatic potential (blue for positive, red for negative, white for hydrophobic and pale blue/red for polar regions). Charges were taken from XPLOR tophcsdx.pro [28]. The views are 90° incremental rotations around the vertical axis. (a) Surface of PnIA, shown in the same orientation as Figure 3. (b) View rotated 90° around the vertical axis. (c) View rotated 180° around the vertical axis. (d) View rotated 270° around the vertical axis. (Figures were generated using GRASP [34].) Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 5 Surface representation of PnIA. Four views of the molecular surface of PnIA, coloured according to electrostatic potential (blue for positive, red for negative, white for hydrophobic and pale blue/red for polar regions). Charges were taken from XPLOR tophcsdx.pro [28]. The views are 90° incremental rotations around the vertical axis. (a) Surface of PnIA, shown in the same orientation as Figure 3. (b) View rotated 90° around the vertical axis. (c) View rotated 180° around the vertical axis. (d) View rotated 270° around the vertical axis. (Figures were generated using GRASP [34].) Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)

Figure 5 Surface representation of PnIA. Four views of the molecular surface of PnIA, coloured according to electrostatic potential (blue for positive, red for negative, white for hydrophobic and pale blue/red for polar regions). Charges were taken from XPLOR tophcsdx.pro [28]. The views are 90° incremental rotations around the vertical axis. (a) Surface of PnIA, shown in the same orientation as Figure 3. (b) View rotated 90° around the vertical axis. (c) View rotated 180° around the vertical axis. (d) View rotated 270° around the vertical axis. (Figures were generated using GRASP [34].) Structure 1996 4, 417-423DOI: (10.1016/S0969-2126(96)00047-0)