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Molecular Dynamics Analysis of Conserved Water Mediated Inter-Domain Recognition of His667-Trp669 in Human Ceruloplasmin

Molecular Dynamics Analysis of Conserved Water Mediated Inter-Domain Recognition of His667-Trp669 in Human Ceruloplasmin

Bishnu Prasad Mukhopadhyay

Bioinformation. 2020 Mar 31;16(3):209-218.

PMID: 32308262

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 moleculardynamics simulation. Results explain the role played by several conserved water centers in the intra and inter-domain recognition throughH-bond interaction with the interacting residues. We observed seventeen conserved water centers in the inter-domain recognition. Weshow that five invariant water centers W13, W14, W18, W23 and W26 connect the Domain 5 to Domain 4 (D5…W…W4). We also show thatfive other water centers W19, W20, W27, W30 and W31 connects the Domain 5 to Domain 6 (D5…W…W6) that is unique in the simulatedform. The W7 and W32 water centers are involved in the D1…W…W6 recognition. This is important for the water-mediated interaction ofGlu1032 to the trinuclear copper cluster present at the interface between these domains. The involvement of W10 water center in theD3…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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1262769878	Isophorone-2,4,4,6,6-d5		1262769-87-8	Price

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