Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the .alpha.-ammonium group binding site of tyrosyl-tRNA synthetase

Biochemistry ◽  
1987 ◽  
Vol 26 (19) ◽  
pp. 6038-6043 ◽  
Author(s):  
Denise M. Lowe ◽  
Greg Winter ◽  
Alan R. Fersht
Keyword(s):  
Binding Site ◽  
Trna Synthetase ◽  
Structure Activity Relationships ◽  
Ammonium Group ◽  
Structure Activity ◽  
Engineered Proteins

scholarly journals Characterization of platinum(II) complexes exhibiting inhibitory activity against the 20S proteasome

2020 ◽  
Vol 7 (8) ◽  
pp. 200545
Author(s):  
Tatsuto Kiwada ◽  
Hiromu Katakasu ◽  
Serina Okumura ◽  
Akira Odani
Keyword(s):  
Inhibitory Activity ◽  
Chemical Structure ◽  
Competitive Inhibition ◽  
Proteasome Inhibitors ◽  
Platinum Complex ◽  
Platinum Complexes ◽  
Binding Mode ◽  
Structure Activity Relationships ◽  
Structure Activity

Proteasome inhibitors are useful for biochemical research and clinical treatment. In our previous study, we reported that the 4N-coordinated platinum complexes with anthracenyl ring and heterocycle exhibited proteasome-inhibitory activity. In the present study, the structure–activity relationships and characterization of these complexes were determined for the elucidation of the role of aromatic ligands. Lineweaver–Burk analysis revealed that the chemical structure of heterocycles affects the binding mode of platinum complexes. Platinum complexes with anthracenyl ring and pyridine showed competitive inhibition, although platinum complexes with anthracenyl ring and phenanthroline showed non-competitive inhibition. The structure–activity relationships demonstrated that anthracenyl moiety plays a crucial role in proteasome-inhibitory activity. The platinum complexes with naphthyl or phenyl rings exhibited lower inhibitory activities than the platinum complex with anthracenyl ring. The reactivity with N-acetylcysteine varied according to the chemical structure of complexes.

Multisubstrate inhibitors of dopamine .beta.-hydroxylase. 2. Structure-activity relationships at the phenethylamine binding site

1987 ◽  
Vol 30 (3) ◽  
pp. 486-494 ◽  
Author(s):  
Lawrence I. Kruse ◽  
Carl Kaiser ◽  
Walter E. DeWolf ◽  
James S. Frazee ◽  
Stephen T. Ross ◽  
...  
Keyword(s):  
Binding Site ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Dopamine Beta Hydroxylase

scholarly journals Identification of the first surrogate agonists for the G protein-coupled receptor GPR132

RSC Advances ◽  
2015 ◽  
Vol 5 (60) ◽  
pp. 48551-48557 ◽  
Author(s):  
Mohamed A. Shehata ◽  
Hanna Belcik Christensen ◽  
Vignir Isberg ◽  
Daniel Sejer Pedersen ◽  
Andreas Bender ◽  
...  
Keyword(s):  
G Protein ◽  
Binding Mode ◽  
Orphan Receptor ◽  
G Protein Coupled Receptor ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
G Protein Coupled

We report the first pharmacological tool agonist for in vitro characterization of the orphan receptor GPR132, preliminary structure–activity relationships based on 32 analogs and a suggested binding mode from docking.

Structural Basis for Understanding Structure−Activity Relationships for the Glutamate Binding Site of the NMDA Receptor

2002 ◽  
Vol 45 (18) ◽  
pp. 3836-3843 ◽  
Author(s):  
Irina G. Tikhonova ◽  
Igor I. Baskin ◽  
Vladimir A. Palyulin ◽  
Nikolai S. Zefirov ◽  
Sergey O. Bachurin
Keyword(s):  
Nmda Receptor ◽  
Binding Site ◽  
Structural Basis ◽  
Structure Activity Relationships ◽  
Glutamate Binding ◽  
Structure Activity

scholarly journals Structural Basis for Understanding Structure−Activity Relationships for the Glutamate Binding Site of the NMDA Receptor.

2002 ◽  
Vol 45 (25) ◽  
pp. 5608-5608 ◽  
Author(s):  
Irina G. Tikhonova ◽  
Igor I. Baskin ◽  
Vladimir A. Palyulin ◽  
Nikolai S. Zefirov ◽  
Sergey O. Bachurin
Keyword(s):  
Nmda Receptor ◽  
Binding Site ◽  
Structural Basis ◽  
Structure Activity Relationships ◽  
Glutamate Binding ◽  
Structure Activity
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