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G protein-coupled receptors (GPCRs) are key pharmaceutical targets in a number of biological diseases and until the recent introduction of Lipidic Cubic Phase (LCP) crystallization, these protein structure have been extremely difficult to solve. LCP crystallization has been successful in solving the structures of a number of GPCRs. However, understanding the process of LCP crystallization is limited. We have studied reconstitution of two native GPCRs, Dopamine 2 Long receptor and Histamine 1 receptor in five different self-assembly lipids; Monoolien (MO), Phytantriol (PT), Phytanoyl monoethanomide (PE), H-farnesoyl monoethanolamide (FE) and Phytanyl Diethanolamide (PDiE). Lipids with the smallest architecture (bilayer thickness and water channel domain) were found to reconstitute these receptors more favourably while MO, the most commonly used lipid in LCP crystallization, was ranked second lowest. We also found incorporation of cholesterol into MO improved GPCR reconstitution.

journal of cytology and molecular biology

﻿Reconstitution of GPCRs in Lipidic Cubic Phase (LCP): Comparison between Human Histamine 1 and Dopamine 2 Long Receptor Reconstitution into Five Different Self-Assembly Lipids﻿

﻿Reconstitution of GPCRs in Lipidic Cubic Phase (LCP): Comparison between Human Histamine 1 and Dopamine 2 Long Receptor Reconstitution into Five Different Self-Assembly Lipids﻿

Reconstitution of GPCRs in Lipidic Cubic Phase (LCP): Comparison between Human Histamine 1 and Dopamine 2 Long Receptor Reconstitution into Five Different Self-Assembly Lipids