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S. Branciamore

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Open access Aug 2026

Interpretable Machine Learning Model of Receptor Dynamics Reveals AT1R Allostery and a Negative Allosteric Modulator

Allosteric modulation of G protein–coupled receptors (GPCRs) offers major advantages in receptor selectivity and signaling control; yet systematic approaches to identify allosteric modulators, define their binding sites, and map the underlying allosteric networks remain limited. Current molecular dynamics (MD) and machine learning (ML)-based methods often rely on correlation-driven or black-box models that provide limited mechanistic insight. We developed an interpretable probabilistic framework that extracts residue-level dependencies from MD ensembles using Bayesian network modeling (BNM). By representing each residue through its local interaction energy, BNM identifies both local and long-range energetic couplings and maps the allosteric communication pathways linking the AngII binding site to the G-protein interface in the angiotensin II type 1 receptor (AT1R). To functionally prioritize these pathways, we integrated BNM with comprehensive mutational analysis, combining whole-receptor alanine mutagenesis data with exhaustive in silico deep mutational scanning to validate BNM-predicted hotspots. This approach recovered state-dependent allosteric communities, revealed residues in noncanonical regions that regulate Gαq coupling and identified positions whose functional importance emerged only with specific, predicted substitutions, as well as highlighted a cryptic intracellular pocket enriched in communication hubs. Guided by these network-derived residues and pocket geometries, structure-based virtual screening identified a small, fragment-like molecule negative allosteric modulator (NAM) named Q2 that attenuates AngII-mediated Gαq signaling. Mutational mapping supports Q2 binding adjacent to the G-protein interface, consistent with its mechanism of action. Together, these results establish a generalizable and interpretable framework for uncovering GPCR allosteric communication networks and discovering modulators that exploit these networks.

Hanyu Chen, Yoon Namkung, Zahra Asadi Jafari et al. · 0 citations
Open access Jul 2026

Protein Frustration Reveals Orthosteric and Allosteric Active Sites in GPCR:G Protein Complexes

The folded structure of a protein is understood to be an optimal energy state. However, previous studies have shown that certain amino acid residue positions that play a critical role in protein function are often in a suboptimal energy state or “frustrated”. Here, we leverage over 1200 three-dimensional structures of G protein-coupled receptors (GPCRs) to demonstrate that residues at the interface between GPCR and its ligand or G protein contain a higher density of frustrated residues compared to other structural regions in the receptor. Likewise, the Gα subunit of the trimeric G proteins shows multiple clusters of highly frustrated residues on its surface that overlap with their effector protein (Gbγ, RGS, Adenylyl cyclase, Ric8) binding interfaces. Our study highlights the use of protein frustration as one of the multiple structural properties to identify protein–protein interfaces and for prospective prediction of potential ligand binding sites.

Wenyuan Wei, Roland Del Mundo, Tianyi Yang et al. · 0 citations
Open access Aug 2026

Integrating molecular dynamics and machine learning to identify potential apo-state conformational and solvent-exposure signatures associated with resistant KRAS mutants

A computational framework integrating molecular dynamics (MD)-derived structural, energetic, thermodynamic, and contact-based descriptors with machine learning may inform the design of inhibitors targeting secondary KRAS resistance mutations, pending validation in additional structurally independent mutant systems.

Katarzyna Mizgalska, Konstancja Urbaniak, Denis Imbody et al. · 0 citations