Modeled structure of trypanothione reductase of Leishmania infantum

被引：32

作者：

Singh, Bishal K. ^{[1
]}

Sarkar, Nandini ^{[1
]}

Jagannadham, M. V. ^{[2
]}

Dubey, Vikash K. ^{[1
]}

机构：

[1] Indian Inst Technol Guwahati, Dept Biotechnol, Gauhati 781039, Assam, India

[2] Banaras Hindu Univ, Inst Med Sci, Mol Biol Unit, Varanasi 221005, Uttar Pradesh, India

来源：

BMB REPORTS | 2008年 / 41卷 / 06期

关键词：

drug design; structure-function; reductase activity; homology Modeling;

D O I：

10.5483/BMBRep.2008.41.6.444

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Trypanothione reductase is an important target enzyme for structure-based drug design against Leishmania. We used homology modeling to construct a three-dimensional structure of the trypanothione reductase (TR) of Leishmania infantum. The structure shows acceptable Ramachandran statistics and a remarkably different active site from glutathione reductase(GR). Thus, a specific inhibitor against TR can be designed without interfering with host (human) GR activity.

引用

页码：444 / 447

页数：4

共 50 条

[1] Biophysical and Folding Parameters of Trypanothione Reductase from Leishmania infantum
Shukla, Anil Kumar
Patra, Sanjukta
Dubey, Vikash Kumar
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2011, 165 (01) : 13 - 23
[2] Inhibition of Leishmania infantum trypanothione reductase by diaryl sulfide derivatives
Saccoliti, Francesco
Angiulli, Gabriella
Pupo, Giovanni
Pescatori, Luca
Madia, Valentina Noemi
Messore, Antonella
Colotti, Gianni
Fiorillo, Annarita
Scipione, Luigi
Gramiccia, Marina
Di Muccio, Trentina
Di Santo, Roberto
Costi, Roberta
Ilari, Andrea
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2017, 32 (01) : 304 - 310
[3] Biophysical and Folding Parameters of Trypanothione Reductase from Leishmania infantum
Anil Kumar Shukla
Sanjukta Patra
Vikash Kumar Dubey
Applied Biochemistry and Biotechnology, 2011, 165
[4] O2-reductase activity of Trypanothione reductase from Leishmania infantum
Malatesta, Francesco
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE, 2014, 34 : S126 - S126
[5] Inhibitory Effect of Silver Nanoparticles on Trypanothione Reductase Activity and Leishmania infantum Proliferation
Baiocco, Paola
Ilari, Andrea
Ceci, Pierpaolo
Orsini, Stefania
Gramiccia, Marina
Di Muccio, Trentina
Colotti, Gianni
ACS MEDICINAL CHEMISTRY LETTERS, 2011, 2 (03): : 230 - 233
[6] Computational Screening for the Identification of Potential Phytochemical Inhibitors of Leishmania infantum Trypanothione Reductase
Bourhia, Mohammed
Shahab, Muhammad
Bouhaissa, Mohamed
Jardan, Yousef A. Bin
Ouahmane, Lahcen
Msanda, Fouad
CHEMISTRYSELECT, 2024, 9 (15):
[7] Efficient Dimerization Disruption of Leishmania infantum Trypanothione Reductase by Triazole-phenyl-thiazoles
Revuelto, Alejandro
de Lucio, Hector
Carlos Garcia-Soriano, Juan
Sanchez-Murcia, Pedro A.
Gago, Federico
Jimenez-Ruiz, Antonio
Camarasa, Maria-Jose
Velazquez, Sonsoles
JOURNAL OF MEDICINAL CHEMISTRY, 2021, 64 (09) : 6137 - 6160
[8] Molecular Docking Studies of Selected Tricyclic and Quinone Derivatives on Trypanothione Reductase of Leishmania infantum
Venkatesan, Santhosh Kannan
Shukla, Anil Kumar
Dubey, Vikash Kumar
JOURNAL OF COMPUTATIONAL CHEMISTRY, 2010, 31 (13) : 2463 - 2475
[9] Small Molecule-Peptide Conjugates as Dimerization Inhibitors of Leishmania infantum Trypanothione Disulfide Reductase
Revuelto, Alejandro
Lopez-Martin, Isabel
de Lucio, Hector
Carlos Garcia-Soriano, Juan
Zanda, Nicola
de Castro, Sonia
Gago, Federico
Jimenez-Ruiz, Antonio
Velazquez, Sonsoles
Camarasa, Maria-Jose
PHARMACEUTICALS, 2021, 14 (07)
[10] Inhibition of Leishmania infantum Trypanothione Reductase by New Aminopropanone Derivatives Interacting with the NADPH Binding Site
Madia, Valentina Noemi
Ialongo, Davide
Patacchini, Elisa
Exertier, Cecile
Antonelli, Lorenzo
Colotti, Gianni
Messore, Antonella
Tudino, Valeria
Saccoliti, Francesco
Scipione, Luigi
Ilari, Andrea
Costi, Roberta
Di Santo, Roberto
MOLECULES, 2023, 28 (01):

← 1 2 3 4 5 →