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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5509
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pubmed:dateCreated |
2001-3-14
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
291
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1793-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11230696-Binding Sites,
pubmed-meshheading:11230696-Crystallography, X-Ray,
pubmed-meshheading:11230696-Endosomes,
pubmed-meshheading:11230696-Humans,
pubmed-meshheading:11230696-Hydrogen Bonding,
pubmed-meshheading:11230696-Lipid Bilayers,
pubmed-meshheading:11230696-Membrane Proteins,
pubmed-meshheading:11230696-Micelles,
pubmed-meshheading:11230696-Models, Molecular,
pubmed-meshheading:11230696-Phosphatidylinositol Phosphates,
pubmed-meshheading:11230696-Protein Conformation,
pubmed-meshheading:11230696-Protein Folding,
pubmed-meshheading:11230696-Protein Structure, Secondary,
pubmed-meshheading:11230696-Protein Structure, Tertiary,
pubmed-meshheading:11230696-Protein Transport,
pubmed-meshheading:11230696-Vesicular Transport Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Structural mechanism of endosome docking by the FYVE domain.
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pubmed:affiliation |
Department of Pharmacology, University of Colorado Health Sciences Center, Denver, CO 80262, USA. tatiana.kutateladze@uchsc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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