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.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code:

Recognizing phosphatidylinositol 3-phosphate

Article Abstract:

The role of lipids in signal transduction with reference to phosphatidylinositol 3-phosphate directing endosomal localization of regulatory proteins is discused. Specific phosphate and hydroxyl group interactions distinguish phosphatidylinositol 3-phosphate from other lipids. The lipid binds to FYVE and PX domains found in intracellular membrane transport/signal transduction proteins and phagocyte proteins, respectively.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code:

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.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code: