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Ectatomin (1eci)

spinqualitylabelsall models 1eci, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Ectatomin (1eci) is the main component of venom of the ant Ectatomma tuberculatum. When bitten by E. tuberculatum, Ectatomin inserts into the target's cell membranes and forms a nonselective cation channel. Structure Biologically, Ectatomin exists as a heterodimer stabilized by disulfide linkages. The α subunit has 37 amino acid residues, while the β subunit has 34 amino acid residues. The structure of Ectatomin was solved using 2D NMR and CHARMm computational optimization, though there are 20 similar proposed conformations. Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a disfulide bond between their hairpin hinge regions. One α-helix from each subunit is kinked, due to the presence of proline residues. The kinked α-helix of the α subunit is more kinked, containing three proline residues, while the kinked α-helix of the β subunit only contains one proline residue. The internal region between the two subunits is primarily composed of hydrophobic residues. Sequence - α subunit GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL Sequence - β subunit WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK