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Abstract
<p class="first" id="d710390e101">There are around 20 Cyclin-dependent kinases (CDKs)
known till date, and various research
groups have reported their role in different types of cancer. The X-ray structures
of some CDKs especially CDK2 was exploited in the past few years, and several inhibitors
have been found, e.g., flavopiridol, indirubicin, roscovitine, etc., but due to the
specificity issues of these inhibitors (binding to all CDKs), these were called as
pan inhibitors. The revolutionary outcome of palbociclib in 2015 as CDK4/6 inhibitor
added a new charm to the specific inhibitor design for CDKs. Computer-aided drug design
(CADD) tools added a benefit to the design and development of new CDK inhibitors by
studying the binding pattern of the inhibitors to the ATP binding domain of CDKs.
Herein, we have attempted a comparative analysis of structural differences between
several CDKs ATP binding sites and their inhibitor specificity by depicting the important
ligand-receptor interactions for a particular CDK to be targeted. This perspective
provides futuristic implications in the design of inhibitors considering the spatial
features and structural insights of the specific CDK.
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