Conformational Landscape and Dynamics of G Protein-Coupled Receptors
Topic Information
Dear Colleagues,
The recent renaissance in X-ray Crystallograpy and Cry-electron Microscopy has led to resolution of many 3-dimensional structures of GPCRs which has significantly elevated our understanding of GPCR activations and functions. This has prompted the development of structure based GPCR virtual drug screening platforms, leading to several candidate agents entering the clinic trials. However, these structure determination tools present limitations as they report on single static states, requirements of thermo-stabilization and homogenous processing which imposes a challenge to gain insights into the continuous conformational transition, allostery and dynamical character of GPCRs. In contrast, to fully understand the receptor function it is critical to probe a complex energy conformational landscape which exhibits the receptor structural heterogeneity and from which the functional diversity is derived. Recently many approaches have accordingly been innovated or upgraded towards this goal.
This Special Issue of Membranes will highlight the significance of gaining insights into the conformational landscape and dynamics of the GPCRs and the state-of-arts approaches that are being utilized for these investigations. It welcomes research articles, opinions, and reviews related to any approaches in advancing our comprehension of the GPCR conformation, allostery, dynamics and signaling, which includes but not limited to nuclear magnetic resonance, mass spectroscopy, electron paramagnetic resonance, single molecule fluorescence, bioluminescent resonance energy transfer, molecular dynamics simulations and other computational methods as well as any derived tactics from these techniques, aiming for progressing our understanding to the plasticity of the GPCR and its functions.
Dr. Libin Ye
Dr. Adnan Sljoka
Topics Editors
Keywords
- membrane proteins
- G protein-coupled receptors
- conformational ensemble
- dynamics
- biophysics
- structural heterogeneity
- plasticity
- signal transduction
- molecular simulations