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Homology model of the CDK1/cyclin B complex

  1. Author:
    McGrath, C. F.
    Pattabiraman, N.
    Kellogg, G. E.
    Lemcke, T.
    Kunick, C.
    Sausville, E. A.
    Zaharevitz, D. W.
    Gussio, R.

  2. Author Address

    NCI, Dev Therapeut Program, Div Canc Treatment & Diagnosis, Frederick, MD 21702 USA. Georgetown Univ, Dept Oncol, Lombardi Comprehens Canc Ctr, Washington, DC 20057 USA. Virginia Commonwealth Univ, Sch Pharm, Inst Struct Biol & Drug Discovery, Dept Med Chem, Richmond, VA 23298 USA. Univ Hamburg, Inst Pharm, Abt Pharmazeut Chem, D-20146 Hamburg, Germany McGrath, CF, NCI, Dev Therapeut Program, Div Canc Treatment & Diagnosis, Frederick, MD 21702 USA
    1. Year: 2005
    2. Date: APR
  2. Journal: Journal of Biomolecular Structure & Dynamics
    1. 22
    2. 5
    3. Pages: 493-502
  4. Type of Article: Article
  1. Abstract:

    We describe a refined homology model of a CDK1/cyclin B complex that was previously used for the structure-based optimization of the Paullone class of inhibitors. The preliminary model was formed from the homologous regions of the deposited CDK2/cyclin A crystal structure. Further refinement of the CDK1/cyclin B complex was accomplished using molecular mechanics and hydropathic analysis with a protocol of constraints and local geometry searches. For the most part, our CKD1/cyclin B homology model is very similar to the high resolution CDK2/cyclin A crystal structure regarding secondary and tertiary features. However, minor discrepancies between the two kinase structures suggest the possibility that ligand design may be specifically tuned for either CDK1 or CDK2. Our examination of the CDK1/cyclin B model includes a comparison with the CDK2/cyclin A crystal structure in the PSTAIRE interface region, connecting portions to the ATP binding domain, as well as the ATP binding site itself

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External Sources

  1. View record in Web of Science®
  2. WOS: 000227504700001

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