Title
Homology modeling and molecular
dynamics simulation study of β carbonic anhydrase of Ascaris
lumbricoides
Authors
Mahima Yadav & Shikha Khandelwal*
Affiliation
Amity Institute of Biotechnology, Amity University Haryana, Gurgaon-122413, India
Shikha Khandelwal - Email: writein.shikha@gmail.com; *Corresponding author
Article Type
Research Article
Date
Received July 12, 2019; Accepted August 12, 2019; Published September 9, 2019
Abstract
Ascaris lumbricoides is the prevalent
parasite causing ascariasis by infecting the human alimentary tract.
This is common in the jejunum of small intestine. Therefore, it is
of interest to describe the target protein β Carbonic Anhydrase
involved in Ascariasis. Carbonic anhydrase (CAs, the metallo
enzymes) is encoded by six evolutionary divergent gene families α,
β, γ, δ, ζ, and η, which contain zinc ion in their catalytic active
site. β-CA is found in plants, algae, fungi, bacteria, protozoans,
arthropods, and nematodes and completely absent in vertebrate
genomes. The absence of β-CA protein in vertebrate makes the enzyme
an important target for inhibitory studies against
helminthic infection. The sequence to function related information
and 3D structure data for β-CA of Ascaris lumbricoides is not
available. Hence, we modeled the 3D structure (using PRIME) for the
molecular dynamics and simulation studies (using the Desmond of
Schrodinger software) and interaction analysis (using STRING
database). The β-CA protein found to be interacting with carbonic
anhydrase protein family along with T27A3, alh13, mtp18, T22F3,
gcy29 proteins. These results provide insights for the understanding
of the functional and biological roles played by β CA. Hence, this
data is useful for the design of drugs for Ascariasis.
Keywords
Ascariasis, carbonic anhydrase, structure analysis, homology modeling, Schrodinger software, molecular dynamics.
Citation
Yadav & Khandelwal et al. Bioinformation 15(8): 572-578 (2019)
Edited by
P Kangueane
ISSN
0973-2063
Publisher
