Prachi Tripathi-Shukla

TL;DR: A strategy for forming and purifying a functional human β2AR–β-arrestin-1 complex is devised that provides a framework for better understanding the basis of GPCR regulation by arrestins.

TL;DR: The crystal structure of β-arrestin-1 in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the human V2 vasopressin receptor is reported, and results indicate a potentially general molecular mechanism for activation of these multifunctional signalling and regulatory proteins.

TL;DR: A surface plasmon resonance biosensor approach is presented that enables, cell- free, label-free, fragment screening that directly measures fragment interactions with wild-type GPCRs and exemplify the method by the discovery of novel, selective, high affinity antagonists of human β2 adrenoceptor.

TL;DR: The functions of the ubiquitous family of G-protein coupled receptors, are mediated and critically modulated by beta arrestins, which bind to phosphorylated receptors and lead to cell reprograming.