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.

Cellular signal transduction, Amino acids, Amino acid structure-activity relationships, Phosphoinositides, Phosphatidylinositols

---

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.

United States, Analysis, Proteins, Protein binding, Structure-activity relationships (Biochemistry), Ubiquitin, Structure

---

Similar abstracts:

• Abstracts: Crystal structure of glycogen synthase kinase 3(beta): structural basis for phosphate-primed substrate specificity and autoinhibition
• Abstracts: Crystal structure of the site-specific recombinase gamma delta resolvase complexed with a 34 bp cleavage site
• Abstracts: Differential requirement for caspase 9 in apoptotic pathways in vivo. Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure
• Abstracts: Calmodulin and munc13 form a Ca(super 2+) sensor/effector complex that controls short-term synaptic plasticity
• Abstracts: Recognition of polyadenylate RNA by the poly(A)-binding protein. U2AF homology motifs: protein recognition in the RRM world

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.