Title
Authors
Bishnu Prasad Mukhopadhyay*
Affiliation
Department of Chemistry, National Institute of Technology-Durgapur, West Bengal, Durgapur –713209, India; *Corresponding author.
Bishnu P Mukhopadhyay Tel.: 0091- 0343 – 2547074; FAX: 0091-0343-2547375 / 2546753; Email address: bpmk2@ch.nitdgp.ac.in. bpmukhopadhyay17@gmail.com
Article Type
Research Article
Date
Received February 19, 2020; Accepted March 5, 2020; Published March 31, 2020
Abstract
The human ceruloplasmin (hCP) is the copper containing ferroxidase enzyme with multifunctional activities (NO-oxidase, NO2-synthase, oxidation of neurotransmitters including antioxidants). Therefore, it is of interest to probe the multi-domain hCP using molecular dynamics simulation. Results explain the role played by several conserved water centers in the intra and inter-domain recognition through H-bond interaction with the interacting residues. We observed seventeen conserved water centers in the inter-domain recognition. We show that five invariant water centers W13, W14, W18, W23 and W26 connect the Domain 5 to Domain 4 (D5···W···W4). We also show that five other water centers W19, W20, W27, W30 and W31 connects the Domain 5 to Domain 6 (D5···W···W6) that is unique in the simulated form. The W7 and W32 water centers are involved in the D1···W···W6 recognition. This is important for the water-mediated interaction of Glu1032 to the trinuclear copper cluster present at the interface between these domains. The involvement of W10 water center in the D3···W10···D4 recognition through Gln552···W10···His667 H-bond interaction is critical in the complexation of CP with myeloperoxidase (Mpo). These observations provide insights to the molecular recognition of hCP with other biomolecules in the system.
Keywords
Conserved water molecules; MD-simulation; Ceruloplasmin.
Citation
Mukhopadhyay, Bioinformation 16(3): 209-218 (2020)
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.
