Computational Prediction of Protein-Protein Interactions of Human Tyrosinase

Su-Fang Wang,Jinhyuk Lee,Sangho Oh,Zhi-Jiang Wang,Guo-Ying Qian,Hong-Yan Han,Yue-Xiu Si

doi:10.1155/2012/192867

Abstract

The various studies on tyrosinase have recently gained the attention of researchers due to their potential application values and the biological functions. In this study, we predicted the 3D structure of human tyrosinase and simulated the protein-protein interactions between tyrosinase and three binding partners, four and half LIM domains 2 (FHL2), cytochrome b-245 alpha polypeptide (CYBA), and RNA-binding motif protein 9 (RBM9). Our interaction simulations showed significant binding energy scores of −595.3 kcal/mol for FHL2, −859.1 kcal/mol for CYBA, and −821.3 kcal/mol for RBM9. We also investigated the residues of each protein facing toward the predicted site of interaction with tyrosinase. Our computational predictions will be useful for elucidating the protein-protein interactions of tyrosinase and studying its binding mechanisms.

Highlights

Tyrosinase (EC 1.14.18.1) is ubiquitously distributed in organisms and is a critical enzyme involved in melanin production, with multiple catalytic functions in pigment production [1,2,3]
Using the same method described for modeling the structure of tyrosinase, we retrieved known homologous structures from the Protein Data Bank (PDB) as follows: 1X4L chain 1 for four and half LIM domains 2 (FHL2) and 2CQ3 chain 1 for RNA-binding motif protein 9 (RBM9)
A previous report revealed that human tyrosinase was highly glycosylated [28,29,30], and it is associated with the correct folding to form the active enzyme

Summary

Introduction

Tyrosinase (EC 1.14.18.1) is ubiquitously distributed in organisms and is a critical enzyme involved in melanin production, with multiple catalytic functions in pigment production [1,2,3]. We modeled the 3D structure of tyrosinase and simulated its protein-protein interactions to understand the structural mechanisms of the binding between tyrosinase and its partners.

Results

Conclusion