We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structural mechanism of endosome docking by the FYVE domain.
- Authors
Kutateladze, T; Overduin, M
- Abstract
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.
- Publication
Science (New York, N.Y.), 2001, Vol 291, Issue 5509, p1793
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.291.5509.1793