Computational prediction for the protein interactions of tyrosinase: protein experimental interactome MAP

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Title
Computational prediction for the protein interactions of tyrosinase: protein experimental interactome MAP
Author(s)
W Wang; D Park; Sunyoung Ji; S J Yin; G Y Qian; H Y Chung; J M Yang; Jinhyuk Lee; Y D Park
Bibliographic Citation
Process Biochemistry, vol. 48, no. 4, pp. 638-648
Publication Year
2013
Abstract
Tyrosinase (EC 1.14.18.1) is a diversely distributed enzyme in various organisms with physiological roles related to pigment production. Tyrosinase has gained the attention of researchers due to its biological functions and potential applications. In this regard, studies on the partner proteins of tyrosinase are important. In this study, we predicted the 3D structure of human tyrosinase and simulated the protein-protein interactions between tyrosinase and binding partners by using the PEIMAP algorithm. As a result, we found that tyrosinase is predicted to bind with G protein-related proteins, potassium voltage-gated channel-related proteins, and vesicle/sorting-related proteins. In particular, GIPC1, GIPC2, GIPC3, TYRP1, and DCT were predicted to primarily bind with tyrosinase. Interacting proteins (103) were secondarily bound to these 5 interacting proteins in the PEIMAP network of tyrosinase. An involvement in melanogenesis was also newly predicted by associating the predicted binding proteins. We simulated the protein-protein bindings by probing the residues of each complex facing toward the predicted site of interaction with tyrosinase. Among the interacting residues, some were predicted to dock to the active site of tyrosinase, which could affect its activity directly. Our computational predictions will be useful for elucidating the protein-protein interactions of tyrosinase and for studying its binding mechanisms and the melanin biosynthesis pathway.
Keyword
InteractomicsProtein-protein interactionSimulationTyrosinasePEIMAP
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.procbio.2013.02.030
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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