We are meeting once a week to do a fast review of the GPCR literature. I have selected to review the Journal of Molecular Biology (JMB), and Cell Journal.

These two journals publish two issues per month, but they also have a just-accepted area where articles are published before an assigned volume is published.

For this week there is no explicit mention of GPCR’s in the Online now area of Cell, or in the Articles in Press area of JMB.

So, that leaves us with just the latest volumes.

[JMB Volume 430, Issue 4]

Dedicated issue on single molecule approaches to “difficult challenges” on folding and dynamics. No specific articles on GPCR’s

There is one quite related review on membrane protein folding studies:

- Applications of Single-Molecule Methods to Membrane Protein Folding Studies
Robert E.Jefferson, Duyoung Min, Karolina Corin, Jing Yang Wang, James U. Bowie
The article can be related to all membrane proteins as it’s written in a completely general way, and there’s specific mention of GPCR’s when talking about oligomerization and force-unfolding. They reference Mathiasen-Kobilka-Stamou et al. 2014, Nature-Methods, who worked with beta2-adrenergic, cannabinoid type I, and opsin. It turns out that with some fitting of FRET signals of reconstituted GPCR’s in proteoliposomes, they estimate a dissociation free-energy of around 4.66 kcal/mol for the beta2-adrenergic receptor. The technique only works for measuring weak interactions, as in the case of GPCR’s oligomers. Later bacteriorhodospsin and other GPCR’s are also mentioned in the context of force-unfolding measurements.

[Cell Volume 172, Issue 4]

- 5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology
Yao Peng, others, Gloriam, Roth, Stevens, Liu
This article comes with a Preview article by Patrick M. Sexton and Arthur Christopoulos contextualizing GPCR Polypharmacology, which they describe as:

“the interaction of a single drug with multiple targets”