7ni4

Human ATM kinase domain with bound M4076 inhibitor

spinqualitylabelsall models 7ni4, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: UGK, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Human checkpoint kinase ataxia telangiectasia-mutated (ATM) plays a key role in initiation of the DNA damage response following DNA double-strand breaks. ATM inhibition is a promising approach in cancer therapy, but, so far, detailed insights into the binding modes of known ATM inhibitors have been hampered due to the lack of high-resolution ATM structures. Using cryo-EM, we have determined the structure of human ATM to an overall resolution sufficient to build a near-complete atomic model and identify two hitherto unknown zinc-binding motifs. We determined the structure of the kinase domain bound to ATPgammaS and to the ATM inhibitors KU-55933 and M4076 at 2.8 A, 2.8 A and 3.0 A resolution, respectively. The mode of action and selectivity of the ATM inhibitors can be explained by structural comparison and provide a framework for structure-based drug design. Molecular basis of human ATM kinase inhibition.,Stakyte K, Rotheneder M, Lammens K, Bartho JD, Gradler U, Fuchss T, Pehl U, Alt A, van de Logt E, Hopfner KP Nat Struct Mol Biol. 2021 Sep 23. pii: 10.1038/s41594-021-00654-x. doi:, 10.1038/s41594-021-00654-x. PMID:34556870 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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