Christoph Parthier

TL;DR: The crystal structure of the complex of human GIP receptor extracellular domain (ECD) with its agonist, the incretin GIP1–42 is reported and the presentation of a well structured, α-helical ligand by the ECD is expected to be conserved among other hormone receptors of this class.

TL;DR: The structural elucidation of several extracellular hormone-binding domains of class B GPCRs in complex with their natural ligands or synthetic analogues reveal similar modes of ligand binding, with concomitant alpha-helical structuring of the ligand.

TL;DR: The X-ray structure with the acceptor aldose d-ribose 5-phosphate (R5P) noncovalently bound in the active site suggests that the sugar is present in multiple forms: in a strained ring-closed beta-d-furanose form in C2-exo conformation as well as in an extended acyclic aldehyde form.

TL;DR: The studies reveal that formation of the central 1,2-dihydroxyethyl-ThDP carbanion-enamine intermediate is thermodynamically favored with increasing carbon chain length of the donor ketose substrate.

TL;DR: The biotechnological generation and biochemical characterization of an oligomer-specific antibody fragment, KW1, and its considerable potential in future studies to detect or inhibit specific types of Aβ conformers are suggested.