ArticlebioRxiv : the preprint server for biology2025
Conformational Dynamics in Insulin Receptor Kinase Reveals a Type III Allosteric Pocket.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Allosteric modulation of kinases is a promising approach for pharmacological intervention, particularly for designing selective kinase modulators. However, the structural information on allosteric pockets remains limited for most kinases in the human kinome. In this work, we present comprehensive characterization of a type III allosteric pocket in the insulin receptor kinase (IRK) by uncovering its structural features and conformational dynamics. Specifically, we used microsecond-scale atomistic molecular dynamics (MD) simulations to investigate apo and inhibitor-bound IRK structures. Our findings suggest that the type III allosteric site is a "back pocket" in IRK, sandwiched between the N-terminal and the C-terminal lobes, beneath the
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