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Barril, X.

Publications and source records attributed to Barril, X..

2 recordsLinked to original sources

Comprehensive detection and characterization of human druggable pockets through novel binding site descriptors

Druggable pockets are protein regions that have the ability to bind organic small molecules, and their characterization is essential in target-based drug discovery. However, strategies to derive pocket descriptors are scarce and usually exhibit limited applicability. Here, we present PocketVec, a novel approach to generate pocket descriptors for any protein binding site of interest through the inverse virtual screening of lead-like molecules. We assess the performance of our descriptors in a variety of scenarios, showing that it is on par with the best available methodologies, while overcoming some important limitations. In parallel, we systematically search for druggable pockets in the folded human proteome, using experimentally determined protein structures and AlphaFold2 models, identifying over 32,000 binding sites in more than 20,000 protein domains. Finally, we derive PocketVec descriptors for each small molecule binding site and run an all-against-all similarity search, exploring over 1.2 billion pairwise comparisons. We show how PocketVec descriptors facilitate the identification of druggable pocket similarities not revealed by structure- or sequence-based comparisons. Indeed, our analyses unveil dense clusters of similar pockets in distinct proteins for which no inhibitor has yet been crystalized, opening the door to strategies to prioritize the development of chemical probes to cover the druggable space.

bioinformatics↗

Are protein-ligand complexes robust structures?

The predominant view in structure-based drug design is that small-molecule ligands, once bound to their target structures, display a well-defined binding mode. While this is convenient from a design perspective, it ignores the fact that structural stability (robustness) is not necessary for thermodynamic stability (binding affinity). In fact, any potential benefit of a rigid binding mode will have to be balanced against the entropic penalty that it entails. Surprisingly, little is known about the causes, consequences and real degree of robustness of protein-ligand complexes. Here we investigate two diverse sets of structures, comprising 79 drug-like and 27 fragment ligands, respectively. We focus on hydrogen bond interactions (469 in total), as they have been described as essential for structural stability. We find that 75% of complexes are anchored by at least one robust hydrogen bond, the remaining 25% either form loose complexes or are constrained by other interactions types. The first type of complexes generally combine a single anchoring point with looser regions, thus balancing order and disorder. Completely constricted protein-ligand complexes are rare and seem to fulfil a functional necessity. Structural stability analysis reveals a hidden layer of complexity in protein-ligand complexes that should be considered in ligand design.

biophysics↗