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Inhibition of (cytosine C5)-methyltransferase by oligonucleotides containing flexible (cyclopentane) and conformationally constrained (bicyclo 3.1.0 hexane) abasic sites

  1. Author:
    Marquez, V. E.
    Wang, P. Y.
    Nicklaus, M. C.
    Maier, M.
    Manoharan, M.
    Christman, J. K.
    Banavali, N. K.
    Mackerell, A. D.

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, Med Chem Lab, Div Basic Sci, Boyles St, Bldg 376, Frederick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, Med Chem Lab, Div Basic Sci, Frederick, MD 21702 USA. ISIS Pharmaceut Inc, Carlsbad, CA 92008 USA. Univ Nebraska, Med Ctr, Dept Biochem & Mol Biol, Omaha, NE 68198 USA. Univ Nebraska, Med Ctr, UNMC, Eppley Canc Ctr, Omaha, NE 68198 USA. Univ Maryland, Sch Pharm, Dept Pharmaceut Sci, Baltimore, MD 21201 USA. Marquez VE NCI, Frederick Canc Res & Dev Ctr, Med Chem Lab, Div Basic Sci, Boyles St, Bldg 376, Frederick, MD 21702 USA.
    1. Year: 2001
  2. Journal: Nucleosides Nucleotides & Nucleic Acids
    1. 20
    2. 4-7
    3. Pages: 451-459
  4. Type of Article: Article
  1. Abstract:

    Pseudorotationally locked sugar analogues based on bicyclo[3.1.0]-hexane templates were placed in DNA duplexes as abasic target sites in the M.HhaI recognition sequence. The binding affinity of the enzyme increases when the abasic site is constrained to the South conformation and decreases when it is constrained to the North conformation. A structural understanding of these differences is provided.

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