• Login
    View Item 
    •   Home
    • UMass Chan Faculty and Staff Research and Publications
    • UMass Chan Faculty and Researcher Publications
    • View Item
    •   Home
    • UMass Chan Faculty and Staff Research and Publications
    • UMass Chan Faculty and Researcher Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of eScholarship@UMassChanCommunitiesPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsThis CollectionPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsProfilesView

    My Account

    LoginRegister

    Help

    AboutSubmission GuidelinesData Deposit PolicySearchingUsage StatisticsAccessibilityTerms of UseWebsite Migration FAQ

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    Publisher version
    View Source
    Access full-text PDFOpen Access
    View Source
    Check access options
    Check access options
    Authors
    Funabashi, Kazumasa
    Sawata, Mizuki
    Nagai, Anna
    Akimoto, Megumi
    Mashimo, Ryutaro
    Takahara, Hidenari
    Kizawa, Kenji
    Thompson, Paul R
    Ite, Kenji
    Kitanishi, Kenichi
    Unno, Masaki
    Show allShow less
    UMass Chan Affiliations
    Thompson Lab
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2021-05-07
    Keywords
    Citrulline
    Inhibitor
    Isozyme
    Post-translational modification
    Quarternary structure
    Selectivity
    Amino Acids, Peptides, and Proteins
    Biochemistry
    Biophysics
    Enzymes and Coenzymes
    Medicinal-Pharmaceutical Chemistry
    Structural Biology
    Show allShow less
    
    Metadata
    Show full item record
    Link to Full Text
    https://doi.org/10.1016/j.abb.2021.108911
    Abstract
    Peptidylarginine deiminase type III (PAD3) is an isozyme belonging to the PAD enzyme family that converts arginine to citrulline residue(s) within proteins. PAD3 is expressed in most differentiated keratinocytes of the epidermis and hair follicles, while S100A3, trichohyalin, and filaggrin are its principal substrates. In this study, the X-ray crystal structures of PAD3 in six states, including its complex with the PAD inhibitor Cl-amidine, were determined. This structural analysis identified a large space around Gly374 in the PAD3-Ca(2+)-Cl-amidine complex, which may be used to develop novel PAD3-selective inhibitors. In addition, similarities between PAD3 and PAD4 were found based on the investigation of PAD4 reactivity with S100A3 in vitro. A comparison of the structures of PAD1, PAD2, PAD3, and PAD4 implied that the flexibility of the structures around the active site may lead to different substrate selectivity among these PAD isozymes.
    Source

    Funabashi K, Sawata M, Nagai A, Akimoto M, Mashimo R, Takahara H, Kizawa K, Thompson PR, Ite K, Kitanishi K, Unno M. Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design. Arch Biochem Biophys. 2021 May 7:108911. doi: 10.1016/j.abb.2021.108911. Epub ahead of print. PMID: 33971157. Link to article on publisher's site

    DOI
    10.1016/j.abb.2021.108911
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/29783
    PubMed ID
    33971157
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1016/j.abb.2021.108911
    Scopus Count
    Collections
    UMass Chan Faculty and Researcher Publications
    Thompson Lab Publications

    entitlement

     
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Lamar Soutter Library, UMass Chan Medical School | 55 Lake Avenue North | Worcester, MA 01655 USA
    Quick Guide | escholarship@umassmed.edu
    Works found in eScholarship@UMassChan are protected by copyright unless otherwise indicated.
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.