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Biology subjects

Apelbaum, A.

Publications and source records attributed to Apelbaum, A..

2 recordsLinked to original sources

Supervised Deep Learning for Efficient Cryo-EM Image Alignment in Drug Discovery with cryoPARES

Cryo-Electron Microscopy (cryo-EM) is a pivotal tool for determining 3D structures of biological macromolecules. Current workflows are computationally demanding and require manual intervention, creating bottlenecks for high-throughput applications like structure-based drug discovery. In such contexts, where all protein samples can be assumed to be equivalent at resolutions relevant for image alignment, information about particle poses from previous refinements could be reused. Existing methods, however, ignore this prior knowledge, aligning each dataset from scratch. We present cryoPARES, a deep learning pose estimation method trained on pre-aligned datasets. Our method not only provides accurate angular predictions significantly faster than traditional approaches but also introduces automated particle pruning capabilities that eliminate manual intervention. Together with its single-pass operation, these features enable near real-time reconstructions that provide feedback during data acquisition. We demonstrate cryoPARESs effectiveness through rapid structural determination of seven ligand-bound complexes across four distinct protein targets. We also release three fragment-bound cryo-EM datasets.

bioinformatics↗

Electron cryo-microscopy structure of the canonical TRPC4 ion channel

Canonical transient receptor channels (TRPC) are non-selective cation channels. They are involved in receptor-operated Ca2+ signaling and have been proposed to act as store-operated channels (SOC). Their malfunction is related to cardiomyopathies and their modulation by small molecules has been shown to be effective against renal cancer cells. The molecular mechanism underlying the complex activation and regulation is poorly understood. Here, we report the electron cryo-microscopy structure of zebrafish TRPC4 in its unliganded (apo), closed state at an overall resolution of 3.6 [A]. The structure reveals the molecular architecture of the cation conducting pore, including the selectivity filter and lower gate. The cytoplasmic domain contains two key hubs that have been shown to interact with modulating proteins. Structural comparisons with other TRP channels give novel insights into the general architecture and domain organization of this superfamily of channels and help to understand their function and pharmacology.

biochemistry↗