Thông tin tài liệu

Full metadata record
DC FieldValueLanguage
dc.contributor.authorManikandan, Amrutha-
dc.date.accessioned2023-11-24T02:15:02Z-
dc.date.available2023-11-24T02:15:02Z-
dc.date.issued2023-
dc.identifier.otherOER000002731vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/23595-
dc.description.abstractThe AMP-activated protein kinase (AMPK) is known to be activated by the protein tyrosine phosphatase non-receptor type 12 (PTP-PEST) under hypoxic conditions. This activation is mediated by tyrosine dephosphorylation of the AMPKα subunit. However, the identity of the phosphotyrosine residues remains unknown. In this study we first predicted the structure of the complex of the AMPKα2 subunit and PTP-PEST catalytic domain using bioinformatics tools and further confirm the stability of the complex using molecular dynamics simulations. Evaluation of the protein-protein interfaces indicates that residue Tyr232 is the most likely site of dephosphorylation on AMPKα2. In addition, we explored the effect of phosphorylation of PTP-PEST residue Tyr64 on the stability of the complex. The phosphorylation of Tyr64, an interface residue, enhances the stability of the complex via the rearrangement of a network of electrostatic interactions in conjunction with conformational changes in the catalytic WPD loop.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2022.05.09.491063v1.full.pdf+htmlvi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherbioRxivvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectNhận dạngvi
dc.subjectTyr232vi
dc.subjectAMPKα2vi
dc.subjectsilicovi
dc.subjectproteinvi
dc.subject.lccTN756vi
dc.titleIn-silico identification of Tyr232 in AMPKα2 as a dephosphorylation site for the protein tyrosine phosphatase PTP-PESTvi
dc.typeJournal articlevi
dc.description.noteCC BY-NC-ND 4.0vi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

Files in This Item:
Thumbnail
  • OER000002731.pdf
      Restricted Access
    • Size : 2,91 MB

    • Format : Adobe PDF



  • This item is licensed under a Creative Commons License Creative Commons