Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/84341
Title: Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study
Authors: Rajesh, Durairaj
Muthukumar, Subramanian
Saibaba, Ganesan
Siva, Durairaj
Akbarsha, Mohammad Abdulkader
Gulyás, Balázs
Padmanabhan, Parasuraman
Archunan, Govindaraju
Keywords: Proteome informatics
Protein–protein interaction networks
Issue Date: 2016
Source: Rajesh, D., Muthukumar, S., Saibaba, G., Siva, D., Akbarsha, M. A., Gulyás, B., et al. (2016). Structural elucidation of estrus urinary lipocalin protein (EULP) and evaluating binding affinity with pheromones using molecular docking and fluorescence study. Scientific Reports, 6, 35900-.
Series/Report no.: Scientific Reports
Abstract: Transportation of pheromones bound with carrier proteins belonging to lipocalin superfamily is known to prolong chemo-signal communication between individuals belonging to the same species. Members of lipocalin family (MLF) proteins have three structurally conserved motifs for delivery of hydrophobic molecules to the specific recognizer. However, computational analyses are critically required to validate and emphasize the sequence and structural annotation of MLF. This study focused to elucidate the evolution, structural documentation, stability and binding efficiency of estrus urinary lipocalin protein (EULP) with endogenous pheromones adopting in-silico and fluorescence study. The results revealed that: (i) EULP perhaps originated from fatty acid binding protein (FABP) revealed in evolutionary analysis; (ii) Dynamic simulation study shows that EULP is highly stable at below 0.45 Å of root mean square deviation (RMSD); (iii) Docking evaluation shows that EULP has higher binding energy with farnesol and 2-iso-butyl-3-methoxypyrazine (IBMP) than 2-naphthol; and (iv) Competitive binding and quenching assay revealed that purified EULP has good binding interaction with farnesol. Both, In-silico and experimental studies showed that EULP is an efficient binding partner to pheromones. The present study provides impetus to create a point mutation for increasing longevity of EULP to develop pheromone trap for rodent pest management.
URI: https://hdl.handle.net/10356/84341
http://hdl.handle.net/10220/41787
ISSN: 2045-2322
DOI: 10.1038/srep35900
Rights: ©The Authors 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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