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X-ray crystallographic analyses of 14 IPMK inhibitor complexes

Wang, H.; Blind, R. D.; Shears, S. B.

2024-05-09 biochemistry
10.1101/2024.05.09.593385 bioRxiv
Show abstract

Inositol polyphosphate multikinase (IPMK) is a ubiquitously expressed kinase that has been linked to several cancers. Here, we report 14 new co-crystal structures (1.7[A] - 2.0[A] resolution) of human IPMK complexed with various IPMK inhibitors developed by another group. The new structures reveal two ordered water molecules that participate in hydrogen-bonding networks, and an unoccupied pocket in the ATP-binding site of human IPMK. New Protein Data Bank (PDB) codes of these IPMK crystal structures are: 8V6W(1.95[A]), 8V6X(1.75[A]), 8V6Y(1.70[A]), 8V6Z(1.85[A]), 8V70(1.85[A]), 8V71(1.70[A]), 8V72(2.0[A]), 8V73(1.90[A]), 8V74(1.85[A]), 8V75(1.85[A]), 8V76(1.95[A]),8V77(1.95[A]), 8V78(1.95[A]), 8V79(1.95[A]).

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