Characterization of the Zinc Binding Site in Methionine Synthase Enzymes ofEscherichia coli:  The Role of Zinc in the Methylation of Homocysteine

1998 ◽  
Vol 120 (33) ◽  
pp. 8410-8416 ◽  
Author(s):  
Katrina Peariso ◽  
Celia W. Goulding ◽  
Sha Huang ◽  
Rowena G. Matthews ◽  
James E. Penner-Hahn
Keyword(s):  
Binding Site ◽  
Ofescherichia Coli ◽  
Methionine Synthase ◽  
Zinc Binding ◽  
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 Characterization of the zinc binding site of bacterial phosphotriesterase.

1992 ◽  
Vol 267 (19) ◽  
pp. 13278-13283 ◽  
Author(s):  
G.A. Omburo ◽  
J.M. Kuo ◽  
L.S. Mullins ◽  
F.M. Raushel
Keyword(s):  
Binding Site ◽  
Zinc Binding ◽  
Zinc Binding Site

scholarly journals Characterization of a novel zinc binding site of protein kinase C inhibitor-1

FEBS Letters ◽  
1991 ◽  
Vol 279 (1) ◽  
pp. 14-18 ◽  
Author(s):  
Ned M. Mozier ◽  
Michael P. Walsh ◽  
James D. Pearson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Site ◽  
Zinc Binding ◽  
Kinase C ◽  
Zinc Binding Site ◽  
Protein Kinase C Inhibitor

scholarly journals Characterization of the Zinc-binding Site of the Histidine-Proline-rich Glycoprotein Associated with Rabbit Skeletal Muscle AMP Deaminase

2002 ◽  
Vol 278 (5) ◽  
pp. 3176-3184 ◽  
Author(s):  
Stefano Mangani ◽  
Wolfram Meyer-Klaucke ◽  
Arthur J. G. Moir ◽  
Maria Ranieri-Raggi ◽  
Daniela Martini ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Binding Site ◽  
Rabbit Skeletal Muscle ◽  
Zinc Binding ◽  
Amp Deaminase ◽  
Zinc Binding Site

Characterization of a Specific, High Affinity [3H]Arginine8Vasopressin-Binding Site on Liver Microsomes from Different Strains of Rat and the Role of Magnesium*

Endocrinology ◽  
1986 ◽  
Vol 118 (3) ◽  
pp. 990-998 ◽  
Author(s):  
VENKAT GOPALAKRISHNAN ◽  
CHRIS R. TRIGGLE ◽  
PRAKASH V. SULAKHE ◽  
J. ROBERT McNEILL
Keyword(s):  
Binding Site ◽  
Liver Microsomes ◽  
High Affinity ◽  
Different Strains

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.

scholarly journals Partial characterization of a binding site for von Willebrand factor on glycocalicin

Blood ◽  
1986 ◽  
Vol 67 (1) ◽  
pp. 19-26 ◽  
Author(s):  
AD Michelson ◽  
J Loscalzo ◽  
B Melnick ◽  
BS Coller ◽  
RI Handin
Keyword(s):  
Binding Site ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Binding Activity ◽  
Proteolytic Fragment ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Beta Galactosidase

The binding of von Willebrand factor (vWF) to platelet membrane glycoprotein Ib (GpIb) facilitates platelet adhesion to vascular subendothelium. In this study, we provide evidence that the vWF binding site is on glycocalicin (GC), a proteolytic fragment of GpIb, and we examine the role of the carbohydrate portion of GC on that binding. The binding to platelets of 6D1, a monoclonal antibody that recognizes an epitope on GpIb and blocks ristocetin-induced vWF binding to platelets, was inhibited by purified GC. In addition, purified GC inhibited ristocetin-dependent binding of 125I-labeled vWF to platelets. Since GC contains 60% carbohydrate by weight, we assessed the role of carbohydrate sequences on its interaction with antibody 6D1 and vWF. Based on the known sequence of the major oligosaccharide chain of GC--N- acetyl neuraminic acid, galactose, N-acetyl glucosamine, N-acetyl galactosamine--we treated GC sequentially with neuraminidase, beta- galactosidase, and beta-N-acetylglucosaminidase. Removal of sialic acid and galactose residues did not affect GC binding. Removal of N-acetyl glucosamine residues did not affect GC binding to 6D1 but did decrease the ability of GC to inhibit vWF binding to platelets, increasing the concentration needed to inhibit binding by 50% (IC50) 40-fold. This suggests that a portion of the oligosaccharide chains on GC contributes to the vWF binding activity of this molecule.

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