Crystal Structures of Human Tissue Kallikrein 4: Activity Modulation by a Specific Zinc Binding Site

2006 ◽  
Vol 362 (5) ◽  
pp. 1094-1107 ◽  
Author(s):  
Mekdes Debela ◽  
Viktor Magdolen ◽  
Valerie Grimminger ◽  
Christian Sommerhoff ◽  
Albrecht Messerschmidt ◽  
...  
Keyword(s):  
Binding Site ◽  
Crystal Structures ◽  
Human Tissue ◽  
Zinc Binding ◽  
Tissue Kallikrein ◽  
Zinc Binding Site ◽  
Kallikrein 4

scholarly journals Crystal Structures of the Mnk2 Kinase Domain Reveal an Inhibitory Conformation and a Zinc Binding Site

Structure ◽  
2005 ◽  
Vol 13 (10) ◽  
pp. 1559-1568 ◽  
Author(s):  
Ralf Jauch ◽  
Stefan Jäkel ◽  
Catharina Netter ◽  
Kay Schreiter ◽  
Babette Aicher ◽  
...  
Keyword(s):  
Binding Site ◽  
Crystal Structures ◽  
Kinase Domain ◽  
Zinc Binding ◽  
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.

Effect of the hydrogen bond network in carbonic anhydrase II zinc binding site. A theoretical study

1998 ◽  
Vol 76 (7) ◽  
pp. 1027-1032 ◽  
Author(s):  
Silvia Álvarez-Santos ◽  
Àngels González-Lafont ◽  
José M Lluch
Keyword(s):  
Hydrogen Bond ◽  
Carbonic Anhydrase ◽  
Binding Site ◽  
Zinc Binding ◽  
Carbonic Anhydrase Ii ◽  
Am1 Method ◽  
Hydrogen Bond Network ◽  
Zinc Binding Site ◽  
Bond Network ◽  
Metal Ligand

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.

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

Characterization of Dimethylargininase from Bovine Brain:  Evidence for a Zinc Binding Site†

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