Crystal structure of Plasmodium falciparum thioredoxin reductase, a validated drug target

2012 ◽  
Vol 425 (4) ◽  
pp. 806-811 ◽  
Author(s):  
Giovanna Boumis ◽  
Giorgio Giardina ◽  
Francesco Angelucci ◽  
Andrea Bellelli ◽  
Maurizio Brunori ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Plasmodium Falciparum ◽  
Drug Target ◽  
Thioredoxin Reductase

Crystal Structure of the Plasmodium falciparum Thioredoxin Reductase–Thioredoxin Complex

2013 ◽  
Vol 425 (18) ◽  
pp. 3446-3460 ◽  
Author(s):  
Karin Fritz-Wolf ◽  
Esther Jortzik ◽  
Michaela Stumpf ◽  
Janina Preuss ◽  
Rimma Iozef ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Plasmodium Falciparum ◽  
Thioredoxin Reductase

Memapsin 2, a drug target for Alzheimer's disease

2003 ◽  
Vol 70 ◽  
pp. 213-220 ◽  
Author(s):  
Gerald Koelsch ◽  
Robert T. Turner ◽  
Lin Hong ◽  
Arun K. Ghosh ◽  
Jordan Tang
Keyword(s):  
Crystal Structure ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Transition State ◽  
Amyloid Precursor Protein ◽  
Therapeutic Target ◽  
Drug Target ◽  
Aspartic Protease ◽  
Precursor Protein ◽  
Memapsin 2

Mempasin 2, a ϐ-secretase, is the membrane-anchored aspartic protease that initiates the cleavage of amyloid precursor protein leading to the production of ϐ-amyloid and the onset of Alzheimer's disease. Thus memapsin 2 is a major therapeutic target for the development of inhibitor drugs for the disease. Many biochemical tools, such as the specificity and crystal structure, have been established and have led to the design of potent and relatively small transition-state inhibitors. Although developing a clinically viable mempasin 2 inhibitor remains challenging, progress to date renders hope that memapsin 2 inhibitors may ultimately be useful for therapeutic reduction of ϐ-amyloid.

Plasmodium falciparum FIKK9.1 is a monomeric serine–threonine protein kinase with features to exploit as a drug target

2021 ◽  
Author(s):  
Anil Kumar D. ◽  
Deepti Shrivastava ◽  
Amogh A. Sahasrabuddhe ◽  
Saman Habib ◽  
Vishal Trivedi
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Kinase ◽  
Drug Target

The hexose transporter of Plasmodium falciparum is a worthy drug target

Acta Tropica ◽  
2004 ◽  
Vol 89 (3) ◽  
pp. 371-374 ◽  
Author(s):  
Thierry Joët ◽  
Sanjeev Krishna
Keyword(s):  
Plasmodium Falciparum ◽  
Drug Target ◽  
Hexose Transporter

Crystal structure of a chimera of human and plasmodium falciparum hypoxanthine guanine phosphoribosyltransferases provides insights into oligomerization

2008 ◽  
Vol 73 (4) ◽  
pp. 1010-1020 ◽  
Author(s):  
P. Gayathri ◽  
I. N. Sujay Subbayya ◽  
Chethan S. Ashok ◽  
T. Senthamizh Selvi ◽  
Hemalatha Balaram ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Plasmodium Falciparum

Crystal Structure of Fully Ligated Adenylosuccinate Synthetase from Plasmodium falciparum

2004 ◽  
Vol 335 (5) ◽  
pp. 1251-1264 ◽  
Author(s):  
K. Eaazhisai ◽  
R. Jayalakshmi ◽  
P. Gayathri ◽  
R.P. Anand ◽  
K. Sumathy ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Plasmodium Falciparum ◽  
Adenylosuccinate Synthetase

scholarly journals The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor

2016 ◽  
Vol 72 (11) ◽  
pp. 813-819 ◽  
Author(s):  
Tony Christopeit ◽  
Ke-Wu Yang ◽  
Shao-Kang Yang ◽  
Hanna-Kirsti S. Leiros
Keyword(s):  
Public Health ◽  
Crystal Structure ◽  
Active Site ◽  
Drug Target ◽  
Zinc Ions ◽  
Clinical Use ◽  
Global Public Health ◽  
Promising Strategy ◽  
Conserved Residue ◽  
Substrate Spectrum

The increasing number of pathogens expressing metallo-β-lactamases (MBLs), and in this way achieving resistance to β-lactam antibiotics, is a significant threat to global public health. A promising strategy to treat such resistant pathogens is the co-administration of MBL inhibitors together with β-lactam antibiotics. However, an MBL inhibitor suitable for clinical use has not yet been identified. Verona integron-encoded metallo-β-lactamase 2 (VIM-2) is a widespread MBL with a broad substrate spectrum and hence is an interesting drug target for the treatment of β-lactam-resistant infections. In this study, three triazolylthioacetamides were tested as inhibitors of VIM-2. One of the tested compounds showed clear inhibition of VIM-2, with an IC50of 20 µM. The crystal structure of the inhibitor in complex with VIM-2 was obtained by DMSO-free co-crystallization and was solved at a resolution of 1.50 Å. To our knowledge, this is the first structure of a triazolylthioacetamide inhibitor in complex with an MBL. Analysis of the structure shows that the inhibitor binds to the two zinc ions in the active site of VIM-2 and revealed detailed information on the interactions involved. Furthermore, the crystal structure showed that binding of the inhibitor induced a conformational change of the conserved residue Trp87.

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