Protein-Protein Interactions in Human Disease, Part A. Advances in Protein Chemistry and Structural Biology, Volume 110. Edited by Rossen Donev. Academic Press. Amsterdam (The Netherlands) and New York: Elsevier. $171.00. xi + 275 p.; ill.; no index. ISBN: 978-0-12-814344-5. 2018.

2018 ◽  
Vol 93 (4) ◽  
pp. 385-385
Author(s):  
Richard B. M. Schasfoort
Keyword(s):  
New York ◽  
The Netherlands ◽  
Structural Biology ◽  
Protein Interactions ◽  
Human Disease ◽  
Protein Chemistry ◽  
Academic Press ◽  
Protein Protein Interactions

scholarly journals Discovery, development and application of drugs targeting BCL-2 pro-survival proteins in cancer

2021 ◽  
Author(s):  
Erinna F. Lee ◽  
W. Douglas Fairlie
Keyword(s):  
Structural Biology ◽  
Protein Interactions ◽  
Basic Science ◽  
Great Success ◽  
Protein Protein Interactions ◽  
New Class ◽  
Success Stories ◽  
History Of ◽  
Approved Drugs ◽  
Close Relatives

The discovery of a new class of small molecule compounds that target the BCL-2 family of anti-apoptotic proteins is one of the great success stories of basic science leading to translational outcomes in the last 30 years. The eponymous BCL-2 protein was identified over 30 years ago due to its association with cancer. However, it was the unveiling of the biochemistry and structural biology behind it and its close relatives’ mechanism(s)-of-action that provided the inspiration for what are now known as ‘BH3-mimetics’, the first clinically approved drugs designed to specifically inhibit protein–protein interactions. Herein, we chart the history of how these drugs were discovered, their evolution and application in cancer treatment.

Structural biology of plant sulfur metabolism: from sulfate to glutathione

2019 ◽  
Vol 70 (16) ◽  
pp. 4089-4103 ◽  
Author(s):  
Joseph M Jez
Keyword(s):  
Structural Biology ◽  
Protein Interactions ◽  
Sulfur Metabolism ◽  
Essential Element ◽  
Glutathione Synthetase ◽  
Protein Protein Interactions ◽  
Glutathione Biosynthesis ◽  
Wide Range ◽  
Aps Reductase ◽  
Level Information

Abstract Sulfur is an essential element for all organisms. Plants must assimilate this nutrient from the environment and convert it into metabolically useful forms for the biosynthesis of a wide range of compounds, including cysteine and glutathione. This review summarizes structural biology studies on the enzymes involved in plant sulfur assimilation [ATP sulfurylase, adenosine-5'-phosphate (APS) reductase, and sulfite reductase], cysteine biosynthesis (serine acetyltransferase and O-acetylserine sulfhydrylase), and glutathione biosynthesis (glutamate-cysteine ligase and glutathione synthetase) pathways. Overall, X-ray crystal structures of enzymes in these core pathways provide molecular-level information on the chemical events that allow plants to incorporate sulfur into essential metabolites and revealed new biochemical regulatory mechanisms, such as structural rearrangements, protein–protein interactions, and thiol-based redox switches, for controlling different steps in these pathways.

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