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- W2296169095 abstract "The dynamics of the ligand-binding domain (LBD) and the intact ionotropic glutamate receptor (iGluR) were studied using Gaussian Network Model (GNM) analysis. The dynamics of LBDs with various allosteric modulators is compared using a novel method of multiple alignment of GNM modes of motion. The analysis reveals that allosteric effectors change the dynamics of amino acids at the upper lobe interface of the LBD dimer as well as at the hinge region between the upper- and lower- lobes. For the intact glutamate receptor the analysis show that the clamshell-like movement of the LBD upper and lower lobes is coupled to the bending of the trans-membrane domain (TMD) helices which may open the channel pore. The results offer a new insight on the mechanism of action of allosteric modulators on the iGluR and support the notion of TMD helices bending as a possible mechanism for channel opening. In addition, the study validates the methodology of multiple GNM modes alignment as a useful tool to study allosteric effect and its relation to proteins dynamics." @default.
- W2296169095 created "2016-06-24" @default.
- W2296169095 creator A5091880796 @default.
- W2296169095 date "2016-01-07" @default.
- W2296169095 modified "2023-10-16" @default.
- W2296169095 title "Dynamics and allostery of the ionotropic glutamate receptors and the ligand binding domain" @default.
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- W2296169095 doi "https://doi.org/10.1002/prot.24977" @default.
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