Increasing the chemical diversity of your drugs
Offering structural insights from mechanistic information
Kinases adopt a variety of conformations to exert their biological role.
Conformational adaptation implies the variation of the size and availability of binding sites, which paves the way for designing drugs with distinct efficiency and selectivity.
High-affinity interactions often entail conformational rearrangements originated by structural changes at the drug-target binding site. Several mechanisms may explain this type of interactions, including compounds capable to induce conformational changes in the target, compounds that bind exclusively to specific conformations, and molecules that forms covalent complexes.
Assessing the parameters that define the steps of the binding mechanism is pivotal for the successful optimization of this kind of compounds.
Enzymlogic determines the binding mechanism of your compounds to the kinase of your interest to provide you with structural information in the early stages of drug discovery.
Features & benefits:
- To obtain structural information when the kinase of your interest cannot be crystallized
- To relate binding mechanism, kinetic parameters and activity to drug structure in the optimization process
- To select and design compounds with non-classical binding to the kinase ATP site
- To determine whether the interaction is simple reversible, reversible with isomerization, reversible with conformational selection or irreversible
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