Computational prediction of protein-protein interactions of human tyrosinase.

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.

SUBMITTER: Wang SF 

PROVIDER: S-EPMC3335181 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature