A systematic study of pleiotropic effects within the receptor responsible for dim-light vision in vertebrates is presented, revealing how light sensitivity can be mediated through differential conformational states of its chromophore and revealing a role for biophysical pleiotropy in shaping the sensory capabilities of receptor proteins.
It is suggested that Gα protein selectivity is an allosterically encoded property of GPCRs and provide a conceptual framework for designing ligands and receptors with tailored Gα protein-biased signaling.
Tegvir S. Boora, Han-Yu Chen, Aaron Cho et al.· bioRxiv· 0 citations
G protein-coupled receptors (GPCRs) mediate a variety of signaling pathways and represent the most common class of pharmaceutical target. While advances in structural biochemistry have provided deep functional insights into key receptors, many of the 800+ human GPCRs remain understudied. We introduce a versatile “deep...
A. Tedman, Muskan Goel, Sohan S. Shah et al.· Nature Communications· 0 citations
This study utilizes a chemical genetic approach to sensitize LRRK2 to existing GTPase inhibitors and shows that pharmacologically engaging the Roc-COR GTPase domain in cells decreases but does not fully inhibit LRRK2-mediated Rab10 T73 phosphorylation.
Rachel E. Prorok, Lawrence Y. Zhu, Vickie Bowcut et al.· bioRxiv· 0 citations
G-protein-coupled receptors (GPCRs) constitute the largest family of membrane proteins involved in cellular signaling. Although X-ray crystallography and cryo-Electron Microscopy (cryo-EM) have provided valuable structural insights into GPCRs, these experimental techniques primarily capture static conformations and can...
Keya Joshi, V. Adediwura, Ying-Long Miao· Frontiers in Chemical Biolog...· 0 citations
Traditional deep mutational scanning (DMS) encodes every single amino-acid substitution from a wild-type sequence. We hypothesize that combinatorial DMS (CDMS) libraries, incorporating all mutations in all combinations, can enable the discovery of high-affinity protein (super)binders by capturing epistatic, non-linear...
Ming-Xuan Jiang, Mo-Han Sun, Nuo Cheng et al.· Molecules and Cells· 0 citations
Cryo-electron microscopy structures of GPR84 in both active and inactive states revealed how different ligands interact with GPR84, influencing its signaling pathways, and provided a structural basis for designing selective modulators of GPR84, which could lead to new therapeutic strategies for diseases involving immun...
Myung Kyung Choi, D. Park, Pankyung Kim et al.· Experimental and Molecular M...· 0 citations
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