Ankita Singhal

TL;DR: The structure of the M257Y/GαCT complex contains the agonist all-trans-retinal covalently bound to the native binding pocket and resembles the G protein binding metarhodopsin-II conformation obtained by the natural activation mechanism; i.e., illumination of the prebound chromophore 11-cis-retINAL.

TL;DR: This work provides the foundation for the development of any mini-G protein and, ultimately, for the structure determination of GPCRs in a fully active state.

TL;DR: A thermostabilization strategy based on systematic mutagenesis coupled to a radioligand-binding thermostability assay that can be applied to receptors, ion channels and transporters and facilitated structure-based drug design applied to GPCRs.

TL;DR: The analysis shows that the CSNB‐causing G90D mutation introduces a salt bridge with K296, which interferes with the E113Q‐K296 activation switch and the covalent binding of the inverse agonist 11‐cis‐retinal, two interactions that are crucial for the deactivation of rhodopsin.

TL;DR: It is shown that the monomeric form of WT rhodopsin and its constitutively active mutants, reconstituted into HDL particles are effectively phosphorylated by GRK1, as well as two more ubiquitously expressed subtypes, GRK2 and GRK5, suggesting that not all phosphorylation sites on rhodopin are equivalent in promoting arrestin-1 binding.