All 10 elements successfully passed this analysis and were thought to be candidate materials that may serve as possible hPKR binders. Next, we focused on an agent of the three FDAapproved visits, which we identified as possible ligands for hPKRs, particularly, Indinavir, Argatroban, and Lapatinib. Figure 9 shows representative types of docking of Indivavir, Argatroban, and Lapatinib for the hPKR1 binding site. As shown, the compounds effectively fill the binding site and are predicted to form specific interactions with elements found to be important for binding of the identified hPKR antagonists, specifically, charged interaction with Glu1192. Hydrogen bonds, and 61 and/or stacking interactions with Arg1443. 32 and Arg3076. 58. Interactions are also formed by these compounds with extra binding site residues, which interact with the binders. Each of the compounds is trusted in the center, and provides well tried and safe compounds which could also exert their actions via hPKRs. The potential cross-reactivity of just one such prospect drug, Indinavir, is further addressed in the.. Prokineticin receptor subtypes 1 and 2 are fresh members of family A GPCRs. Prokineticins and their receptors play essential roles under various physiological problems, and blocking PKRs may serve as a therapeutic tool for various pathologies, including inflammation, circadian rhythm disturbances, severe pain, and cancer. In this study, we extracted necessary functional groups from small molecule PKR antagonists which were previously reported, using structure activity relationship examination, and we used them in a virtual screening method. Consequently, we could identify several possible PKR ligands with novel scaffolds. Apparently, the electronic visits involved many HIV protease inhibitors that are discussed next when it comes to recognized side effects and potential new indications of the drugs. Computational docking of known ligands to the numerous template 3D model of a PKRs structure enabled us to estimate ligand receptor connections and provided a structural explanation of the significance of the chemical features we obtained in the analysis of known PKR binders. Homology modeling of the hPKR docking and subtypes of identified small molecule antagonists In this study we modeled the 3D structure of the hPKR subtypes and explored the relationships formed between hPKR1 and small molecule binders. Our computational investigation unveiled that hPKR1 is predicted to possess a TM bunch binding site, capable of binding little molecule ligands, similarly to other GPCR family A people, such as the receptors. This does occur despite the proven fact that the receptors endogenous ligands are relatively large proteins, which almost certainly bind the extra-cellular surface of the receptors. The latter is demonstrated in experimental information on Kallmann syndrome mutations.