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
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

2013 ◽  
Vol 9 (2) ◽  
pp. e1002909 ◽  
Author(s):  
Thomas Stockner ◽  
Therese R. Montgomery ◽  
Oliver Kudlacek ◽  
Rene Weissensteiner ◽  
Gerhard F. Ecker ◽  
...  

2003 ◽  
Vol 278 (46) ◽  
pp. 45325-45332 ◽  
Author(s):  
Jean-Francois Collet ◽  
Jonathan Conrad D'Souza ◽  
Ursula Jakob ◽  
James C. A. Bardwell

2009 ◽  
Vol 285 (5) ◽  
pp. 3271-3281 ◽  
Author(s):  
Ho-Won Kang ◽  
Iuliia Vitko ◽  
Sang-Soo Lee ◽  
Edward Perez-Reyes ◽  
Jung-Ha Lee

2018 ◽  
Vol 116 (2) ◽  
pp. 528-533 ◽  
Author(s):  
Ivan B. Lomakin ◽  
Sergey E. Dmitriev ◽  
Thomas A. Steitz

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.


1998 ◽  
Vol 76 (7) ◽  
pp. 1027-1032 ◽  
Author(s):  
Silvia Álvarez-Santos ◽  
Àngels González-Lafont ◽  
José M Lluch

The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carbonic anhydrase II, Zn2+ metalloenzyme ligands.


Biochemistry ◽  
1998 ◽  
Vol 37 (14) ◽  
pp. 4791-4798 ◽  
Author(s):  
Ralf Bogumil ◽  
Markus Knipp ◽  
Sibylle M. Fundel ◽  
Milan Vašák

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