Preparation, Properties and Analysis of a Zinc Ion-Binding Protein from the Benign Hypertrophic Human Prostate Gland

1973 ◽  
Vol 1 (1) ◽  
pp. 104-105
Author(s):  
M. JOAN REED ◽  
S. R. STITCH ◽  
J. G. HEATHCOTE ◽  
R. J. WASHINGTON
Keyword(s):  
Binding Protein ◽  
Prostate Gland ◽  
Zinc Ion ◽  
Human Prostate ◽  
Ion Binding ◽  
Zinc Ion Binding

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.

Models for protein-zinc ion binding sites. II. The catalytic sites

2001 ◽  
Vol 83 (3-4) ◽  
pp. 150-165 ◽  
Author(s):  
David W. Deerfield ◽  
Charles W. Carter ◽  
Lee G. Pedersen
Keyword(s):  
Binding Sites ◽  
Zinc Ion ◽  
Ion Binding ◽  
Catalytic Sites ◽  
Ion Binding Sites ◽  
Zinc Ion Binding

Affinity capillary electrophoresis study of the linkage existing between proton and zinc ion binding to bacitracin A1

2003 ◽  
Vol 24 (5) ◽  
pp. 801-807 ◽  
Author(s):  
Massimo Castagnola ◽  
Diana Valeria Rossetti ◽  
Rosanna Inzitari ◽  
Alberto Vitali ◽  
Alessandro Lupi ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
Zinc Ion ◽  
Ion Binding ◽  
Affinity Capillary Electrophoresis ◽  
Zinc Ion Binding

scholarly journals A ratiometric fluorescent molecular probe with enhanced two-photon response upon Zn2+ binding for in vitro and in vivo bioimaging

2014 ◽  
Vol 5 (9) ◽  
pp. 3469-3474 ◽  
Author(s):  
Kizhmuri P. Divya ◽  
Sivaramapanicker Sreejith ◽  
Pichandi Ashokkumar ◽  
Kang Yuzhan ◽  
Qiwen Peng ◽  
...  
Keyword(s):  
Zinc Ion ◽  
Molecular Probe ◽  
Ion Binding ◽  
Ion Imaging ◽  
Two Photon ◽  
Zinc Ion Binding

The ratiometric two-photon (2P) probe GBC shows enhanced 2P activity upon zinc ion binding and has been used for zinc ion imaging in vitro and in vivo.

Unravelling the inhibitory zinc ion binding site and the metal exchange mechanism in human DPP III

2021 ◽  
Author(s):  
Antonija Tomić ◽  
Hrvoje Brkić ◽  
Antonia Matić ◽  
Sanja Tomić
Keyword(s):  
Binding Site ◽  
Dipeptidyl Peptidase ◽  
Zinc Ion ◽  
Exchange Mechanism ◽  
Ion Binding ◽  
Metal Exchange ◽  
Human Tissues ◽  
Protein Catabolism ◽  
Almost All ◽  
Zinc Ion Binding

Dipeptidyl peptidase III (DPP III), a zinc-dependent exopeptidase, is widely distributed in organisms and present in almost all human tissues. In addition to its involvement in protein catabolism, it plays...

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