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| FAS-associating death domain-containing protein ： ウィキペディア英語版 |
FADD
Fas-Associated protein with Death Domain (FADD), also called MORT1, is encoded by the ''FADD'' gene on the 11q13.3 region of chromosome 11 in humans.
FADD is an adaptor protein that bridges members of the tumor necrosis factor receptor superfamily, such as the Fas-receptor, to procaspases 8 and 10 to form the death-inducing signaling complex (DISC) during apoptosis. As well as its most well known role in apoptosis, FADD has also been seen to play a role in other processes including proliferation, cell cycle regulation and development.
==Structure==
FADD is a 23 kDa protein, made up of 280 amino acids. It contains two main domains: a C terminal death domain (DD) and an N terminal death effector domain (DED). Each domain, although sharing very little sequence similarity, are structurally similar to one another, with each consisting of 6 α helices. The DD of FADD binds to receptors such as the Fas receptor at the plasma membrane via their DD. The interaction between the death domains are electrostatic interactions involving α helices 2 and 3 of the 6 helix domain. The DED binds to the DED of intracellular molecules such as procaspase 8. It is thought that this interaction occurs through hydrophobic interactions.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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