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Computational prediction for the protein interactions of tyrosinase: Protein experimental interactome MAP
Authors:Wei Wang  Daeui Park  Sunyoung Ji  Shang-Jun Yin  Guo-Ying Qian  Hae Young Chung  Jun-Mo Yang  Jinhyuk Lee  Yong-Doo Park
Affiliation:1. College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China;2. Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University, Busan 609-735, Korea;3. Korean Bioinformation Center (KOBIC), Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea;4. Department of Bioinformatics, University of Sciences and Technology, Daejeon 305-350, Korea;5. Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center, Seoul 135-710, Korea;6. Yangtze Delta Region Institute of Tsinghua University, Jiaxing 314006, Zhejiang, PR China
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.
Keywords:Tyrosinase  Simulation  Protein–protein interaction  PEIMAP  Interactomics  PPI"  },{"  #name"  :"  keyword"  ,"  $"  :{"  id"  :"  kw0035"  },"  $$"  :[{"  #name"  :"  text"  ,"  _"  :"  protein–protein interaction  PEIMAP"  },{"  #name"  :"  keyword"  ,"  $"  :{"  id"  :"  kw0045"  },"  $$"  :[{"  #name"  :"  text"  ,"  _"  :"  protein experimental interactome map
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