IDEAS home Printed from https://ideas.repec.org/a/adp/jctbeb/v4y2017i1p9-11.html
   My bibliography  Save this article

Allosteric regulation in drug design

Author

Listed:
  • Ashfaq Ur Rehman

    (State Key Laboratory of Microbial Metabolism, Department of Bioinformatics and Biostatistics, China
    Department of Biochemistry, Abdul Wali Khan University Mardan, Pakistan)

  • Shah Saud

    (Laboratory of Analytical Biochemistry and Bio separation, Shanghai Jiao Tong University, China)

  • Nasir Ahmad

    (Department of Chemistry, Islama College University Peshawar, Pakistan)

  • Abdul Wadood

    (Department of Biochemistry, Abdul Wali Khan University Mardan, Pakistan)

  • R Hamid

    (Department of Bioinformatics, Muhammad Ali Jinnah University Islamabad, Pakistan)

Abstract

Protein and enzymes play significant roles in biological processes of all living organisms; their functions are regulated through allosteric mechanism, which are initiated through attachment of ligand or inhibitors with the protein or enzymes other than active (orthosteric) sites. This mini review involved mechanism, types and importance of allosteric regulations in drug design process.

Suggested Citation

  • Ashfaq Ur Rehman & Shah Saud & Nasir Ahmad & Abdul Wadood & R Hamid, 2017. "Allosteric regulation in drug design," Current Trends in Biomedical Engineering & Biosciences, Juniper Publishers Inc., vol. 4(1), pages 9-11, May.
    • Handle: RePEc:adp:jctbeb:v:4:y:2017:i:1:p:9-11
    DOI: 10.19080/CTBEB.2017.04.555630
    as

    Download full text from publisher

    File URL: https://juniperpublishers.com/ctbeb/pdf/CTBEB.MS.ID.555630.pdf
    Download Restriction: no
    File URL: https://juniperpublishers.com/ctbeb/CTBEB.MS.ID.555630.php
    Download Restriction: no
    File URL: https://libkey.io/10.19080/CTBEB.2017.04.555630?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. John Kuriyan & David Eisenberg, 2007. "The origin of protein interactions and allostery in colocalization," Nature, Nature, vol. 450(7172), pages 983-990, December.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yalbi Itzel Balderas-Martínez & Michael Savageau & Heladia Salgado & Ernesto Pérez-Rueda & Enrique Morett & Julio Collado-Vides, 2013. "Transcription Factors in Escherichia coli Prefer the Holo Conformation," PLOS ONE, Public Library of Science, vol. 8(6), pages 1-9, June.
    2. Robert Kalescky & Hongyu Zhou & Jin Liu & Peng Tao, 2016. "Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery," PLOS Computational Biology, Public Library of Science, vol. 12(4), pages 1-21, April.

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:adp:jctbeb:v:4:y:2017:i:1:p:9-11. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Robert Thomas (email available below). General contact details of provider: .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.