Faculty Opinions recommendation of Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.

2021 ◽  
Author(s):  
Daniel Hebert
Keyword(s):  
Domain Motions

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

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.

scholarly journals Cryo-EM structures reveal coordinated domain motions that govern DNA cleavage by Cas9

2019 ◽  
Vol 26 (8) ◽  
pp. 679-685 ◽  
Author(s):  
Xing Zhu ◽  
Ryan Clarke ◽  
Anupama K. Puppala ◽  
Sagar Chittori ◽  
Alan Merk ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Domain Motions

scholarly journals Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein

2017 ◽  
Vol 139 (27) ◽  
pp. 9246-9258 ◽  
Author(s):  
Daryl Good ◽  
Charlie Pham ◽  
Jacob Jagas ◽  
Józef R. Lewandowski ◽  
Vladimir Ladizhansky
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Small Amplitude ◽  
Helical Protein ◽  
Domain Motions
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