Investigating Sec14 Domain Lipid Binding using Structural Modeling

Modeling Lipid Binding in SEC14 proteins using Patellin1 (PATL1)

Structural and Functional Assessment of Perilipin 2 Lipid Binding Domain(s)

Although perilipin 2 (Plin2) has been shown to bind lipids with high affinity, the Plin2 lipid binding site has yet to be defined. This is of interest since Plin2's affinity for lipids has been suggested to be important for lipid droplet biogenesis and intracellular triacylglycerol accumulation. To define these regions, mouse Plin2 and several deletion mutants expressed as recombinant proteins ...

Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes.

Dimeric tubulin, an abundant water-soluble cytosolic protein known primarily for its role in the cytoskeleton, is routinely found to be associated with mitochondrial outer membranes, although the structure and physiological role of mitochondria-bound tubulin are still unknown. There is also no consensus on whether tubulin is a peripheral membrane protein or is integrated into the outer mitochon...

The Lipid-binding Domain of Wild Type and Mutant -Synuclein

-Synuclein ( S) is linked to Parkinson disease through its deposition in an amyloid fibril formwithin Lewy Body deposits, and by the existence of three S point mutations that lead to early onset autosomal dominant Parkinsonism. The normal function of S is thought to be linked to the ability of the protein to bind to the surface of synaptic vesicles. Upon binding to vesicles, S undergoes a struc...

Structural basis of nSH2 regulation and lipid binding in PI3Kα

We report two crystal structures of the wild-type phosphatidylinositol 3-kinase α (PI3Kα) heterodimer refined to 2.9 Å and 3.4 Å resolution: the first as the free enzyme, the second in complex with the lipid substrate, diC4-PIP₂, respectively. The first structure shows key interactions of the N-terminal SH2 domain (nSH2) and iSH2 with the activation loop that suggest a mechanism by which the en...