HOME   |    PDF   |   


Molecular dynamics analysis of conserved water mediated inter-domain recognition of His667-Trp669 in human ceruloplasmin



Bishnu Prasad Mukhopadhyay*



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



Received February 19, 2020; Accepted March 5, 2020; Published March 31, 2020



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 (D5WW4). We also show that five other water centers W19, W20, W27, W30 and W31 connects the Domain 5 to Domain 6 (D5WW6) that is unique in the simulated form. The W7 and W32 water centers are involved in the D1WW6 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 D3W10D4 recognition through Gln552W10His667 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.



Conserved water molecules; MD-simulation; Ceruloplasmin.



Mukhopadhyay, Bioinformation 16(3): 209-218 (2020)


Edited by

P Kangueane






Biomedical Informatics



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.