Pinning Down Viral Proteins: A New Prototype for Virus–Host Cell Interaction

Pin 1 is an enzyme that specifically catalyzes the cis–trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by...

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Detalles Bibliográficos
Autores principales: Kojima, Yoshitsugu, Ryo, Akihide
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2010
Materias:
Microbiology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3125566/
https://www.ncbi.nlm.nih.gov/pubmed/21738521
http://dx.doi.org/10.3389/fmicb.2010.00107
Descripción
Sumario:Pin 1 is an enzyme that specifically catalyzes the cis–trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by a host factor Pin1. Pin1 is now positioned as an important modulator of the molecular crosstalk between virus and host cells and could be a unique target for anti-virus therapy. This new type of post-translational modification by Pin1 might be involved in the regulation of other viral proteins.

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