scholarly journals Mutational Analysis of the High-Affinity Zinc Binding Site Validates a Refined Human Dopamine Transporter Homology Model

2013 ◽  
Vol 9 (2) ◽  
pp. e1002909 ◽  
Author(s):  
Thomas Stockner ◽  
Therese R. Montgomery ◽  
Oliver Kudlacek ◽  
Rene Weissensteiner ◽  
Gerhard F. Ecker ◽  
...  
Keyword(s):  
Binding Site ◽  
Dopamine Transporter ◽  
Mutational Analysis ◽  
Homology Model ◽  
Zinc Binding ◽  
High Affinity ◽  
Zinc Binding Site

scholarly journals Construction of a High Affinity Zinc Binding Site in the Metabotropic Glutamate Receptor mGluR1

2000 ◽  
Vol 276 (13) ◽  
pp. 10110-10118 ◽  
Author(s):  
Anders A. Jensen ◽  
Paul O. Sheppard ◽  
Liselotte B. Jensen ◽  
Patrick J. O'Hara ◽  
Hans Bräuner-Osborne
Keyword(s):  
Binding Site ◽  
Glutamate Receptor ◽  
Metabotropic Glutamate Receptor ◽  
Zinc Binding ◽  
Metabotropic Glutamate ◽  
High Affinity ◽  
Zinc Binding Site

scholarly journals Occupancy of the zinc-binding site by transition metals decreases the substrate affinity of the human dopamine transporter by an allosteric mechanism.

2017 ◽  
Vol 292 (17) ◽  
pp. 7161-7161
Author(s):  
Yang Li ◽  
Felix P. Mayer ◽  
Peter S. Hasenhuetl ◽  
Verena Burtscher ◽  
Klaus Schicker ◽  
...  
Keyword(s):  
Transition Metals ◽  
Binding Site ◽  
Dopamine Transporter ◽  
Zinc Binding ◽  
Substrate Affinity ◽  
Allosteric Mechanism ◽  
Zinc Binding Site

scholarly journals Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site

2003 ◽  
Vol 278 (46) ◽  
pp. 45325-45332 ◽  
Author(s):  
Jean-Francois Collet ◽  
Jonathan Conrad D'Souza ◽  
Ursula Jakob ◽  
James C. A. Bardwell
Keyword(s):  
Oxidative Stress ◽  
Binding Site ◽  
Zinc Binding ◽  
High Affinity ◽  
Zinc Binding Site ◽  
Thioredoxin 2

scholarly journals Structural Determinants of the High Affinity Extracellular Zinc Binding Site on Cav3.2 T-type Calcium Channels

2009 ◽  
Vol 285 (5) ◽  
pp. 3271-3281 ◽  
Author(s):  
Ho-Won Kang ◽  
Iuliia Vitko ◽  
Sang-Soo Lee ◽  
Edward Perez-Reyes ◽  
Jung-Ha Lee
Keyword(s):  
Calcium Channels ◽  
Binding Site ◽  
Zinc Binding ◽  
Structural Determinants ◽  
High Affinity ◽  
Zinc Binding Site

scholarly journals Occupancy of the Zinc-binding Site by Transition Metals Decreases the Substrate Affinity of the Human Dopamine Transporter by an Allosteric Mechanism

2017 ◽  
Vol 292 (10) ◽  
pp. 4235-4243 ◽  
Author(s):  
Yang Li ◽  
Felix P. Mayer ◽  
Peter S. Hasenhuetl ◽  
Verena Burtscher ◽  
Klaus Schicker ◽  
...  
Keyword(s):  
Transition Metals ◽  
Binding Site ◽  
Dopamine Transporter ◽  
Zinc Binding ◽  
Substrate Affinity ◽  
Allosteric Mechanism ◽  
Zinc Binding Site

scholarly journals Biomimetic Nanostructures: Creating a High-Affinity Zinc-Binding Site in a Folded Nonbiological Polymer

2008 ◽  
Vol 130 (27) ◽  
pp. 8847-8855 ◽  
Author(s):  
Byoung-Chul Lee ◽  
Tammy K. Chu ◽  
Ken A. Dill ◽  
Ronald N. Zuckermann
Keyword(s):  
Binding Site ◽  
Zinc Binding ◽  
High Affinity ◽  
Zinc Binding Site

scholarly journals Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation

2018 ◽  
Vol 116 (2) ◽  
pp. 528-533 ◽  
Author(s):  
Ivan B. Lomakin ◽  
Sergey E. Dmitriev ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Translation Initiation ◽  
Zinc Ion ◽  
Zinc Binding ◽  
Ion Binding ◽  
Binding Interface ◽  
Zinc Binding Site ◽  
Reading Frames ◽  
Zinc Ion Binding

The density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein support noncanonical translation initiation, promote translation reinitiation on a specific set of mRNAs with short upstream reading frames, and regulate ribosome recycling. DENR and MCT-1 form a heterodimer, which binds to the ribosome. We determined the crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR at 2.0-Å resolution. The structure of the heterodimer reveals atomic details of the mechanism of DENR and MCT-1 interaction. Four conserved cysteine residues of DENR (C34, C37, C44, C53) form a classical tetrahedral zinc ion-binding site, which preserves the structure of the DENR’s MCT-1–binding interface that is essential for the dimerization. Substitution of all four cysteines by alanine abolished a heterodimer formation. Our findings elucidate further the mechanism of regulation of DENR-MCT-1 activities in unconventional translation initiation, reinitiation, and recycling.

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