Next new MolTag paper from MedUni


First authored by Ralph Gradisch with support by Marco Niello

After 2.5 years within his PhD and joining a completely new research field in computational biophysics Ralph Gradisch and co-authors (as Marco Niello from the Sitte-group) elucidated how a substrate e.g. serotonin mediates conformational changes in the respective transporter leading to transporter occlusion. This expands the knowledge of previously published structures of the human serotonin transporter. Additionally they propose that water is a key player within this process.

The publication has been first appeard in the Journal of Biological Chemistry (JBC) online on Jan 20, 2022.

Occlusion of the human serotonin transporter is mediated by serotonin-induced conformational changes in the bundle domain

Ralph Gradisch, Dániel Szöllösi, Marco Niello, Erika Lazzarin, Harald H. Sitte, Thomas Stockner


Collective motions of hSERT in response to 5HT binding. Principal component analyses of the 20 trajectories were used to identify conformational changes. A) The largest motion (principal component 1; PC1) is a rotation of TM1b, TM2 and TM6a of the bundle domain. B) PC2 is a rotation of the bundle domain helices, mainly TM1b, TM6a and TM7, perpendicular to PC1. Projection of all trajectories (color code as in Figure 2) onto PC1 and PC2 for the 5HT-bound hSERT simulations C) that remain open, D) that reach the intermediate state, or E) that fully occlude. Panel F) shows all 10 5HT-free trajectories projected onto the same common PC1 and PC2.

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