Optical Spectroscopy of Biomolecular Dynamics

Vöhringer, Peter; Haran, Gilad

doi:10.1002/cphc.200400287

Cited by 2 publications

(2 citation statements)

References 15 publications

(14 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Movies were analyzed using SPARTAN analysis software 44 . Individual traces were smoothed using a nonlinear filter 45 with the following filter parameters: window = 2, M = 2 and P = 15. Each experiment was performed ≥4 times to ensure reproducibility.…”

Section: Methodsmentioning

confidence: 99%

Homo- and hetero-dimeric subunit interactions set affinity and efficacy in metabotropic glutamate receptors

Habrian,

Latorraca,

et al. 2023

Nat Commun

View full text Add to dashboard Cite

Metabotropic glutamate receptors (mGluRs) are dimeric class C G-protein–coupled receptors that operate in glia and neurons. Glutamate affinity and efficacy vary greatly between the eight mGluRs. The molecular basis of this diversity is not understood. We used single-molecule fluorescence energy transfer to monitor the structural rearrangements of activation in the mGluR ligand binding domain (LBD). In saturating glutamate, group II homodimers fully occupy the activated LBD conformation (full efficacy) but homodimers of group III mGluRs do not. Strikingly, the reduced efficacy of Group III homodimers does not arise from differences in the glutamate binding pocket but, instead, from interactions within the extracellular dimerization interface that impede active state occupancy. By contrast, the functionally boosted mGluR II/III heterodimers lack these interface ‘brakes’ to activation and heterodimer asymmetry in the flexibility of a disulfide loop connecting LBDs greatly favors occupancy of the activated conformation. Our results suggest that dimerization interface interactions generate substantial functional diversity by differentially stabilizing the activated conformation. This diversity may optimize mGluR responsiveness for the distinct spatio-temporal profiles of synaptic versus extrasynaptic glutamate.

show abstract

Section: Methodsmentioning

confidence: 99%

Homo- and hetero-dimeric subunit interactions set affinity and efficacy in metabotropic glutamate receptors

Habrian,

Latorraca,

et al. 2023

Nat Commun

View full text Add to dashboard Cite

show abstract

“…It was conceived following a recent German-Israeli conference, [1] and can be seen as an informal "status report" on the field. An influential review written in 1991 stated that "Studies of biomolecular dynamics today are in some sense where atomic physics was near 1885.…”

mentioning

confidence: 99%