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Human P2Y(6) receptor: Molecular modeling leads to the rational design of a novel agonist based on a unique conformational preference

  1. Author:
    Costanzi, S.
    Joshi, B. V.
    Maddileti, S.
    Mamedova, L.
    Gonzalez-Moa, M. J.
    Marquez, V. E.
    Harden, T. K.
    Jacobson, K. A.

  2. Author Address

    NIDDK, Computat Chem Core Lab & Mol Recognit Sect, NIH, DHHS, Bethesda, MD 20892 USA. Univ N Carolina, Sch Med, Dept Pharmacol, Chapel Hill, NC 27599 USA. NCI, Med Chem Lab, NIH, DHHS, Frederick, MD 21702 USA Costanzi, S, NIDDK, Computat Chem Core Lab & Mol Recognit Sect, NIH, DHHS, Bethesda, MD 20892 USA
    1. Year: 2005
    2. Date: DEC 29
  2. Journal: Journal of Medicinal Chemistry
    1. 48
    2. 26
    3. Pages: 8108-8111
  4. Type of Article: Article
  1. Abstract:

    Combining molecular dynamics (MD) in a hydrated phospholipid (DOPC) bilayer, a Monte Carlo search, and synthesis of locked nucleotide analogues, we discovered that the Southern conformation of the ribose is preferred for ligand recognition by the P2Y(6) receptor. 2'-Deoxy-(S)-methanocarbaUDP was found to be a full agonist of the receptor and displayed a 10-fold higher potency than that for the corresponding flexible 2'-deoxyUDP. MD results also suggested a conformational change of the second extracellular loop consequent to agonist binding

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  1. View record in Web of Science®
  2. WOS: 000234301800002

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