Importance of inter-residue interactions in ligand-receptor binding
Apstrakt
In the present study, the role of inter-residue interactions in ligand binding and the ligand-receptor interactions were examined. Computational chemistry methods of ligand docking and molecular dynamics simulations were used to study the binding of beta-funaltrexamine (beta-FNA) and N-methyl-beta-funaltrexamine (N-methyl-beta-FNA) to mu- and kappa-opioid receptors and to the mu-receptor with Lys303(6.58) Glu mutation. It was found that inter-residue interactions Lys233(5.39)-Glu303(6.58) in the mutant receptor and Lys227(5.39) Asp223(5.35) in the.-receptor are more likely to prevent covalent bond formation between beta-FNA and the receptor than the ligand-receptor interactions. This emphasizes the importance of inter-residue interactions in ligand binding as well as the effects of point-mutations. (C) 2016 Institute of Chemistry, Slovak Academy of Sciences
Ključne reči:
inter-residue interactions / opioid receptors / molecular docking / molecular dynamics / beta-funaltrexamineIzvor:
Chemical Papers, 2016, 70, 7, 994-1002Finansiranje / projekti:
DOI: 10.1515/chempap-2016-0017
ISSN: 0366-6352
WoS: 000379757200013
Scopus: 2-s2.0-84959018672
Kolekcije
Institucija/grupa
VinčaTY - JOUR AU - Senćanski, Milan V. AU - Došen-Mićović, Ljiljana I. PY - 2016 UR - https://vinar.vin.bg.ac.rs/handle/123456789/1181 AB - In the present study, the role of inter-residue interactions in ligand binding and the ligand-receptor interactions were examined. Computational chemistry methods of ligand docking and molecular dynamics simulations were used to study the binding of beta-funaltrexamine (beta-FNA) and N-methyl-beta-funaltrexamine (N-methyl-beta-FNA) to mu- and kappa-opioid receptors and to the mu-receptor with Lys303(6.58) Glu mutation. It was found that inter-residue interactions Lys233(5.39)-Glu303(6.58) in the mutant receptor and Lys227(5.39) Asp223(5.35) in the.-receptor are more likely to prevent covalent bond formation between beta-FNA and the receptor than the ligand-receptor interactions. This emphasizes the importance of inter-residue interactions in ligand binding as well as the effects of point-mutations. (C) 2016 Institute of Chemistry, Slovak Academy of Sciences T2 - Chemical Papers T1 - Importance of inter-residue interactions in ligand-receptor binding VL - 70 IS - 7 SP - 994 EP - 1002 DO - 10.1515/chempap-2016-0017 ER -
@article{ author = "Senćanski, Milan V. and Došen-Mićović, Ljiljana I.", year = "2016", abstract = "In the present study, the role of inter-residue interactions in ligand binding and the ligand-receptor interactions were examined. Computational chemistry methods of ligand docking and molecular dynamics simulations were used to study the binding of beta-funaltrexamine (beta-FNA) and N-methyl-beta-funaltrexamine (N-methyl-beta-FNA) to mu- and kappa-opioid receptors and to the mu-receptor with Lys303(6.58) Glu mutation. It was found that inter-residue interactions Lys233(5.39)-Glu303(6.58) in the mutant receptor and Lys227(5.39) Asp223(5.35) in the.-receptor are more likely to prevent covalent bond formation between beta-FNA and the receptor than the ligand-receptor interactions. This emphasizes the importance of inter-residue interactions in ligand binding as well as the effects of point-mutations. (C) 2016 Institute of Chemistry, Slovak Academy of Sciences", journal = "Chemical Papers", title = "Importance of inter-residue interactions in ligand-receptor binding", volume = "70", number = "7", pages = "994-1002", doi = "10.1515/chempap-2016-0017" }
Senćanski, M. V.,& Došen-Mićović, L. I.. (2016). Importance of inter-residue interactions in ligand-receptor binding. in Chemical Papers, 70(7), 994-1002. https://doi.org/10.1515/chempap-2016-0017
Senćanski MV, Došen-Mićović LI. Importance of inter-residue interactions in ligand-receptor binding. in Chemical Papers. 2016;70(7):994-1002. doi:10.1515/chempap-2016-0017 .
Senćanski, Milan V., Došen-Mićović, Ljiljana I., "Importance of inter-residue interactions in ligand-receptor binding" in Chemical Papers, 70, no. 7 (2016):994-1002, https://doi.org/10.1515/chempap-2016-0017 . .