Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity

Detalhes bibliográficos
Autor(a) principal: Tang,Hongmin
Data de Publicação: 2015
Outros Autores: Zhou,Peifu
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000400547
Resumo: 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.
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spelling Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase ActivityMolecular chaperoneHspa5tyrosinasemelaninmelanosomeIn 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.Instituto de Tecnologia do Paraná - Tecpar2015-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000400547Brazilian Archives of Biology and Technology v.58 n.4 2015reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-8913201500462info:eu-repo/semantics/openAccessTang,HongminZhou,Peifueng2015-10-26T00:00:00Zoai:scielo:S1516-89132015000400547Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-10-26T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
title Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
spellingShingle Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
Tang,Hongmin
Molecular chaperone
Hspa5
tyrosinase
melanin
melanosome
title_short Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
title_full Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
title_fullStr Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
title_full_unstemmed Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
title_sort Heat Shock Protein Hspa5 Interacts with and Protects Tyrosinase Activity
author Tang,Hongmin
author_facet Tang,Hongmin
Zhou,Peifu
author_role author
author2 Zhou,Peifu
author2_role author
dc.contributor.author.fl_str_mv Tang,Hongmin
Zhou,Peifu
dc.subject.por.fl_str_mv Molecular chaperone
Hspa5
tyrosinase
melanin
melanosome
topic Molecular chaperone
Hspa5
tyrosinase
melanin
melanosome
description 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.
publishDate 2015
dc.date.none.fl_str_mv 2015-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000400547
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000400547
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-8913201500462
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.58 n.4 2015
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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