Xin Gu

TL;DR: The crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin is determined by serial femtosecond X-ray laser crystallography and provides a basis for understanding GPCR-mediated arrestin-biased signalling.

TL;DR: It is shown that the major interactions between activated rhodopsin and Gi are mediated by the C-terminal helix of the Gi α-subunit, which is wedged into the cytoplasmic cavity of the transmembrane helix bundle and directly contacts the amino terminus of helix 8 of rhodopin.

TL;DR: Low-resolution crystal structures of the human α1β2γ1 holo-AMPK complex bound to its allosteric modulators AMP and the glycogen-mimic cyclodextrin are presented to illustrate an underlying mechanism ofallosteric AMPK modulation by AMp and glycogen, whose binding changes the equilibria between alternate AID (AMP) and carbohydrate-binding module (glycogen) interactions.

TL;DR: Sequence alignments and structure-based mutagenesis indicate that this mode of corepressor binding is highly conserved in a large set of transcriptional repressors, thus providing a general mechanism for gene repression mediated by the TPL family of core Pressors.

TL;DR: The crystal structure of Norrin is reported, which reveals a unique dimeric structure with each monomer adopting a conserved cystine knot fold, which provides crucial insights into the assembly and activation of the Norrin-Fz4-Lrp5/6 signaling complex.