Marcus J. Swann

TL;DR: The ability of α-Syn to sense lipid packing defects and to remodel membrane structure supports its proposed role in vesicle trafficking.

TL;DR: The biophysical characterization of protein–ligand interactions in solution using techniques such as thermal shift assay, or on surfaces using, for example, dual polarization interferometry, plays an increasingly important role in complementing crystal structure determinations.

TL;DR: The results indicate that, whereas the calmodulin dependent enzymatic domain is restricted to the amino-terminal residues 1–384 of CyaA, the membrane-interacting, translocation-competent domain extends up to residue 489, which suggests an important role of the region adjacent to the catalytic domain of CyA in promoting its interaction with and its translocation across the plasma membrane of target cells.

TL;DR: The bent structure provides a molecular rationale for the susceptibility of IgE-Fc ϵRI complexes to allergenic stimulation and is critical for FcϵRI-mediated IgE activity.