Pascal Egloff

TL;DR: This work purified three neurotensin-bound NTR1 variants from Escherichia coli and determined their X-ray structures at up to 2.75 Å resolution using vapor diffusion crystallization experiments, and provided a structural rationale for the long-known effects of C-terminal palmitoylation reactions on G protein–coupled receptor signaling, receptor maturation, and desensitization.

TL;DR: An in vitro selection platform based on synthetic single domain antibodies named sybodies, designed to target the limited hydrophilic surfaces of membrane proteins, and designed three sybody libraries that exhibit different shapes and moderate hydrophobicity of the randomized surface.

TL;DR: This protocol describes in vitro procedures for generation of synthetic single-domain antibodies called ‘sybodies’, which can be engineered to target specific protein conformations, labile membrane proteins or protein complexes.

TL;DR: The results demonstrate how the plasticity of a common protein fold can contribute to the recognition and control of antagonists by an innate defence mechanism, whereby the monovalency of the lectin for its ligand implies a novel mechanism of lectin-mediated toxicity.

TL;DR: This study studied the internal mobility of a G-protein α subunit in its apo and nucleotide-bound forms and characterized their dynamical features at multiple time scales using solution NMR, small-angle X-ray scattering, and molecular dynamics simulations to demonstrate that the conformational plasticity of G proteins is a central feature of their switching functionality.