Domain motions accompanying tet repressor induction defined by changes of interspin distances at selectively labeled sites

1999 ◽  
Vol 292 (4) ◽  
pp. 945-946
Author(s):  
B. Tiebel ◽  
N. Radzwill ◽  
L.M. Aung-Hilbrich ◽  
V. Helbl ◽  
H.J. Steinhoff ◽  
...  
Keyword(s):  
Tet Repressor ◽  
Interspin Distances ◽  
Domain Motions

Domain motions accompanying tet repressor induction defined by changes of interspin distances at selectively labeled sites 1 1Edited by N. Baumeister

1999 ◽  
Vol 290 (1) ◽  
pp. 229-240 ◽  
Author(s):  
Beatrix Tiebel ◽  
Nicole Radzwill ◽  
Lwin Mar Aung-Hilbrich ◽  
Vera Helbl ◽  
Heinz-Jürgen Steinhoff ◽  
...  
Keyword(s):  
Tet Repressor ◽  
Interspin Distances ◽  
Domain Motions

scholarly journals Evolutionary Basis for the Coupled-domain Motions inThermus thermophilusLeucyl-tRNA Synthetase

2009 ◽  
Vol 284 (15) ◽  
pp. 10088-10099 ◽  
Author(s):  
Kristina Mary Ellen Weimer ◽  
Brianne Leigh Shane ◽  
Michael Brunetto ◽  
Sudeep Bhattacharyya ◽  
Sanchita Hati
Keyword(s):  
Trna Synthetase ◽  
Domain Motions

scholarly journals Sodium Binding Stabilizes the Outward-Open State of SERT by Limiting Bundle Domain Motions

Cells ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 255
Author(s):  
Dániel Szöllősi ◽  
Thomas Stockner
Keyword(s):  
Substrate Binding ◽  
Chloride Ion ◽  
Synaptic Cleft ◽  
High Concentration ◽  
Neurologic Diseases ◽  
Presynaptic Nerve Terminal ◽  
Access Path ◽  
Outer Vestibule ◽  
Dynamics Simulations ◽  
Domain Motions

The human serotonin transporter (hSERT) removes the neurotransmitter serotonin from the synaptic cleft by reuptake into the presynaptic nerve terminal. A number of neurologic diseases are associated with dysfunction of the hSERT, and several medications for their treatment are hSERT blockers, including citalopram, fluoxetine, and paroxetine. The substrate transport is energized by the high concentration of external NaCl. We showed through molecular dynamics simulations that the binding of NaCl stabilized the hSERT in the substrate-binding competent conformation, which was characterized by an open access path to the substrate-binding site through the outer vestibule. Importantly, the binding of NaCl reduced the dynamics of the hSERT by decreasing the internal fluctuations of the bundle domain as well as the movement of the bundle domain relative to the scaffold domain. In contrast, the presence of only the bound chloride ion did not reduce the high domain mobility of the apo state.

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