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  • Electronic Resource  (2)
  • 1995-1999  (2)
  • 1
    Electronic Resource
    Electronic Resource
    A model for the binding of low molecular weight inhibitors to the active site of thrombin (1999)
    Springer
    Journal of computer aided molecular design 13 (1999), S. 579-588 
    Details
    ISSN: 1573-4951
    Keywords: anti-thrombotics ; conformational searching ; molecular mechanics ; X-ray coordinates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract This paper describes the construction, validation and application of an active site model of the serine protease thrombin. Initial use was made of medium resolution X-ray crystallographic structures of thrombin complexed with low molecular weight, non-specific inhibitors to create a computationally useable active site shell of the enzyme. Molecular mechanics methods were then applied to dock known ligands into the active site region in order to derive a model that would accurately predict binding conformations. Validation of the modelling process was achieved by comparison of the predicted enzyme-bound conformations with their known, crystallographic binding conformations. The resultant model was used extensively for predictive purposes prior to obtaining confirmatory crystal data relating to a ligand possessing a novel and unexpected binding component complexed to thrombin. The data served both to confirm the accuracy of the binding site model and to provide information for the further refinement of the model.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008098615891
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Modelling study of protein kinase inhibitors: Binding mode of staurosporine and origin of the selectivity of CGP 52411 (1995)
    Springer
    Journal of computer aided molecular design 9 (1995), S. 465-472 
    Details
    ISSN: 1573-4951
    Keywords: EGF-receptor kinase ; Docking ; Adenosine triphosphate ; Bioactive conformation ; Dianilinophthalimides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A model for the binding mode of the potent protein kinase inhibitor staurosporine is proposed. Using the information provided by the crystal structure of the cyclic-AMP-dependent protein kinase, it is suggested that staurosporine, despite a seemingly unrelated chemical structure, exploits the same key hydrogen-bond interactions as ATP, the cofactor of the protein kinases, in its binding mode. The structure-activity relationships of the inhibitor and a docking analysis give strong support to this protein tyrosine kinase is rationalized on the basis of the model. It is proposed that this selectivity originates in the occupancy, by one of the anilino moieties of the inhibitor, of the region of the enzyme cleft that normally binds the ribose ring of ATP, which appears to possess a marked lipophilic character in this kinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00124317
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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