Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
Article Abstract:
The FYVE domains' interaction with the phosphatidylinositol three-phosphate membranes controls membrane trafficking and signalling pathways. Study of the FYVE domain structure revealed that this amino acid region is composed of two antiparallel beta sheets and an L helix stabilized by two Zn2+-binding clusters. It was also observed that the tip of the FYVE domain has basic and hydrophobic surfaces that promote nonspecific interactions with the phospholipid bilayer.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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Mechanism of ubiquitin recognition by the CUE domain of Vps9p
Article Abstract:
The CUE domain of the Vps9p sorting protein binds to monoubiquitin. The two binding surfaces of the CUE monomer are opposite to each other and cannot bind a ubiquitin molecule simultaneously. However, dimerization facilitates both sides to bind a monoubiquitin molecule.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
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