@misc{Khachatryan_Hamlet_Systematic,
 author={Khachatryan, Hamlet},
 address={Երևան},
 howpublished={online},
 publisher={ՀՀ ԳԱԱ հրատ.},
 abstract={Human Immunodeficiency Virus-1 protease (HIV-1 PR) is among the most extensively studied drug targets in the Protein Data Bank (PDB), with more than 600 structural models predominantly derived by X-ray crystallography. This study presents a comprehensive analysis of the binding-site conformational space across the available structural record: 690 crystal structures deposited in the PDB with ≥90% sequence identity and resolution better than or equal to 2.50 Å, of which 684 were successfully featurized by pipeline. The structural dataset covers wild-type enzyme, crystallographic stabilization mutants, drug-resistant variants, and 452 distinct inhibitor binders. Each binding site was featurized as a volume-filling point cloud with six descriptors (electrostatic potential, lipophilicity, and pharmacophoric features) and represented as a geodesic distance matrix with further embedding in spectral distance space. Affinity propagation clustered all pockets into 16 discrete conformational states, with four dominant states accounting for 85% of all structures.},
 title={Systematic Analysis of the HIV-1 Protease Active-Site Conformational Space Across 690 Crystal Structures},
 type={Հանդես},
 keywords={Biology},
}