http://www.cnr.it/ontology/cnr/individuo/prodotto/ID298812
Computational Comparison of Imidazoline Association with the I2 Binding Site in Human Monoamine Oxidases (vol 54, pg 1200, 2014) (Articolo in rivista)
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- Label
- Computational Comparison of Imidazoline Association with the I2 Binding Site in Human Monoamine Oxidases (vol 54, pg 1200, 2014) (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/ci5003747 (literal)
- Alternative label
Basile, Livia; Pappalardo, Matteo; Guccione, Salvatore; Milardi, Danilo; Ramsay, Rona R. (2014)
Computational Comparison of Imidazoline Association with the I2 Binding Site in Human Monoamine Oxidases (vol 54, pg 1200, 2014)
in Journal of chemical information and modeling
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Basile, Livia; Pappalardo, Matteo; Guccione, Salvatore; Milardi, Danilo; Ramsay, Rona R. (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- +Etnalead s.r.l., c/o EtnaBuilding, Scuola Superiore di Catania, Universita? degli Studi di Catania, via S. Nullo 5/i, I-95123 Catania,
Italy
?Dipartimento di Scienze Chimiche, Universita?degli Studi di Catania, Viale A.Doria 6 Ed.3, Citta?Universitaria, I- 95125 Catania, Italy
§Dipartimento di Scienze del Farmaco, Universita?degli Studi di Catania, Viale A.Doria 6 Ed. 2, Citta?Universitaria, I-95125 Catania,
Italy
?IBB-CNR, Istituto di Biostrutture e Bioimmagini, UOS di Catania c/o Dipartimento di Scienze Chimiche, Universita?degli Studi di
Catania, Viale A.Doria 6 Ed.3, Citta? Universitaria, I- 95125 Catania, Italy
?Biomedical Sciences Research Complex, University of St. Andrews, North Haugh, St. Andrews KY16 8QP, U.K. (literal)
- Titolo
- Computational Comparison of Imidazoline Association with the I2 Binding Site in Human Monoamine Oxidases (vol 54, pg 1200, 2014) (literal)
- Abstract
- Imidazoline ligands in I2-type binding sites in the brain alter
monoamine turnover and release. One example of an I2 binding site
characterized by binding studies, kinetics, and crystal structure has been
described in monoamine oxidase B (MAO B). MAO A also binds imidazolines
but has a different active site structure. Docking and molecular dynamics were
used to explore how 2-(2-benzofuranyl)-2-imidazoline hydrochloride (2-BFI)
binds to MAO A and to explain why tranylcypromine increases tight binding to
MAO B. The energy for 2-BFI binding to MAO A was comparable to that for
tranylcypromine-modified MAO B, but the location of 2-BFI in the MAO A
could be anywhere in the monopartite substrate cavity. Binding to the
tranylcypromine-modified MAO B was with high affinity and in the entrance
cavity as in the crystal structure, but the energies of interaction with the native
MAO B were less favorable. Molecular dynamics revealed that the entrance
cavity of MAO B after tranylcypromine modification is both smaller and less flexible. This change in the presence of
tranylcypromine may be responsible for the greater affinity of tranylcypromine-modified MAO B for imidazoline ligands. (literal)
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