Adaptin

spinqualitylabelsall models Structure of Adaptin core: AP-α-2 (cyan), AP-β-1 (magenta), AP-μ-1 (green), AP-σ-1 (olive) complex with inositole hexakisphosphate (PDB entry 2vgl) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Adaptin (AP) are proteins which mediate the formation of vescicles by clathrin-coated pits. The AP-2 complex is a heterotetramer composed a core domain containing 2 large AP: AP-α or AP-γ and AP-β, a medium-size AP: AP-μ and small AP: AP-σ, 2 appendage domains or EAR. The core domain binds to the membrane and to cargo proteins which should be internalized and the EAR domains bind to clathrin and accessory proteins. There are different AP complexes in mammals. Adaptin core: AP-α-2, AP-β-1, AP-μ-1, AP-σ-1 complex with inositole hexakisphosphate. Inositole hexakisphosphate binding site (2vgl). The AP-1 complex heterotetramer μ subunit packages insulin receptor substrates into clathrin-coated vescicles. This is needed for insulin/insulin-like growth factor bioactivities including mitogenesis. The AP-3 complex heterotetramer is involved in the biogenesis of lysosome-related organelles. It contains subunits β3, μ3, δ and σ3. The AP-4 complex heterotetramer is involved in the targeting proteins from the trans-Golgi network (TGN) to yhr endosomal-lysosomal system. It contains subunits β-type, μ-type, ε and σ-type. 3D structures of adaptin Adaptin 3D structures

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