Structural mechanism of endosome docking by the FYVE domain
T Kutateladze, M Overduin - Science, 2001 - science.org
Science, 2001•science.org
The recruitment of trafficking and signaling proteins to membranes containing
phosphatidylinositol 3-phosphate [PtdIns (3) P] is mediated by FYVE domains. Here, the
solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the
free state was compared with the structures of the domain complexed with PtdIns (3) P and
mixed micelles. The multistep binding mechanism involved nonspecific insertion of a
hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket …
phosphatidylinositol 3-phosphate [PtdIns (3) P] is mediated by FYVE domains. Here, the
solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the
free state was compared with the structures of the domain complexed with PtdIns (3) P and
mixed micelles. The multistep binding mechanism involved nonspecific insertion of a
hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket …
The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.
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