Proteomics

Dataset Information

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A rapid, tag-free way to purify functional GPCRs


ABSTRACT: A GPCR purification method is described based on how the Galpha-CT (alpha5 helix) interacts with G-protein coupled receptors (GPCRs). The importance of this region in binding to and stabilizing the active GPCR state (R*) is well established, as it plays a conserved role in allosterically linking R* binding to Gα activation. Although only about 20 amino acids, the Galpha-CT contributes approximately 50% of the total interacting surface area with active receptors (R*). Galpha-CT binding also activates the G protein, by triggering conformational changes in the Galpha subunit that facilitate GDP – GTP exchange and heterotrimer dissociation.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Cercopithecus Aethiops (green Monkey) (grivet)

SUBMITTER: Phillip Wilmarth  

LAB HEAD: David Farrens, Ph.D.

PROVIDER: PXD046070 | Pride | 2024-05-22

REPOSITORIES: Pride

Dataset's files

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Farrens_lower__band_20230413_OE.msf Msf
Farrens_lower__band_20230413_OE.raw Raw
Farrens_upper__band_20230413_OE.msf Msf
Farrens_upper__band_20230413_OE.raw Raw
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Publications

A rapid, tag-free way to purify functional GPCRs.

Shumate Anthony D AD   Farrens David L DL  

The Journal of biological chemistry 20231212 1


G protein-coupled receptors (GPCRs) play diverse signaling roles and represent major pharmaceutical targets. Consequently, they are the focus of intense study, and numerous advances have been made in their handling and analysis. However, a universal way to purify GPCRs has remained elusive, in part because of their inherent instability when isolated from cells. To address this, we have developed a general, rapid, and tag-free way to purify GPCRs. The method uses short peptide analogs of the Gα s  ...[more]

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