Structural mechanism of endosome docking by the FYVE domain

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Structural mechanism of endosome docking by the FYVE domain. / Kutateladze, TG; Overduin, Michael.

In: Science, Vol. 291, 02.03.2001, p. 1793-1796.

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Kutateladze, TG ; Overduin, Michael. / Structural mechanism of endosome docking by the FYVE domain. In: Science. 2001 ; Vol. 291. pp. 1793-1796.

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@article{3d8c07745d55400b88e6af5eeb21c77d,
title = "Structural mechanism of endosome docking by the FYVE domain",
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.",
author = "TG Kutateladze and Michael Overduin",
year = "2001",
month = mar
day = "2",
doi = "10.1126/science.291.5509.1793",
language = "English",
volume = "291",
pages = "1793--1796",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",

}

RIS

TY - JOUR

T1 - Structural mechanism of endosome docking by the FYVE domain

AU - Kutateladze, TG

AU - Overduin, Michael

PY - 2001/3/2

Y1 - 2001/3/2

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0035793903&partnerID=8YFLogxK

U2 - 10.1126/science.291.5509.1793

DO - 10.1126/science.291.5509.1793

M3 - Article

C2 - 11230696

VL - 291

SP - 1793

EP - 1796

JO - Science

JF - Science

SN - 0036-8075

ER -