|
Title |
Molecular docking analysis of UniProtKB nitrate reductase enzyme with known natural flavonoids
|
|
Authors |
Ayub Shaik1, Vishnu Thumma2, Aruna
Kumari Kotha2, Sandhya Kramadhati2, Jalapathy
|
|
Affiliation |
1Department of Chemistry, University
College of Science, Osmania University, Hyderabad, Telangana, India;
2 Department of Sciences and Humanities, Matrusri Engineering
College, Hyderabad, Telangana, India; 3Bioinformatics Division,
Osmania University, Hyderabad,
|
|
|
Seshagiri Bandi – E-mail: giri.bandi@gmail.com
|
|
Article Type |
Hypothesis
|
|
Date |
Received October 21, 2016; Accepted November 11, 2016; Published December 27, 2016
|
|
Abstract |
The functional inference of UniProtKB nitrate reductase enzyme (UniProtKB - P0AF33) through structural modeling is of interest in plant biology. Therefore, a homology model for UniProtKB variant of the enzyme was constructed using available data with the MODELER software tool. The model was further docked with five natural flavonoid structures such as hesperetin, naringenin, leucocyanidin, quercetin and hesperetin triacetate using the AUTODOCK (version 4.2) software tool. The structure aided molecular interactions of these flavonoids with nitrate reductase is documented in this study. The binding features (binding energy (ΔG) value, H bonds and docking score) hesperetin to the enzyme model is relatively high, satisfactory and notable. This data provides valuable insights to the relative binding of several naturally occurring flavonoids to nitrate reductase enzyme and its relevance in plant biology.
|
|
Keywords |
Homology modeling, nitrate reductase, natural flavonoids, docking
|
|
Citation |
Shaik et al. Bioinformation 12(12): 425-429 (2016)
|
|
Edited by |
P Kangueane
|
|
ISSN |
0973-2063
|
|
Publisher |
|
|
License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
|