| Revue: | Brazilian archives of biology and technology |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000387721 |
| ISSN: | 1516-8913 |
| Autores: | Tang, Hongmin1 Zhou, Peifu1 |
| Instituciones: | 1Guizhou Minzu University, College of Chemistry & Environmental Science, Guiyang. China |
| Año: | 2015 |
| Periodo: | Jul-Ago |
| Volumen: | 58 |
| Número: | 4 |
| Paginación: | 547-552 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | In this study, heat shock protein, Hspa5 was cloned, expressed and purified subsequently confirmed that it interacted with the tyrosinase (TYR) in vitro. Then, using the crystal structure of the homologous protein from the bacteria as a template, a homology model of human TYR was constructed. This model was further applied to investigate the molecular docking with Hspa5. The model showed that the interaction between the TYR and Hspa5 was mainly maintained by some hydrogen bonds in a quite low energy state. The results indicated that TYR was protected in different denaturation conditions by Hspa5. It was concluded that Hspa5 served as a molecular chaperone of TYR, which could help to better understand the molecule regulation mechanism of TRY in many kinds of diseases |
| Disciplinas: | Química |
| Palabras clave: | Bioquímica, Proteínas de choque térmico, Chaperonas moleculares, Protección química, Tirosinasa, Melanina, Melanosomas |
| Keyword: | Chemistry, Biochemistry, Heat shock proteins, Molecular chaperone, Chemical protection, Tyrosinase, Melanin, Melanosomes |
| Texte intégral: | Texto completo (Ver HTML) |
