7NI6
Human ATM kinase with bound ATPyS
Summary for 7NI6
| Entry DOI | 10.2210/pdb7ni6/pdb |
| Related | 7NI4 7NI5 |
| EMDB information | 12343 12345 12346 12347 12350 12351 12352 |
| Descriptor | Serine-protein kinase ATM, ZINC ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | kinase, inhibitor, dna damage response, cancer research, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 710278.30 |
| Authors | Stakyte, K.,Rotheneder, M.,Lammens, K.,Bartho, J.D. (deposition date: 2021-02-11, release date: 2021-09-01, Last modification date: 2024-07-10) |
| Primary citation | Stakyte, K.,Rotheneder, M.,Lammens, K.,Bartho, J.D.,Gradler, U.,Fuchss, T.,Pehl, U.,Alt, A.,van de Logt, E.,Hopfner, K.P. Molecular basis of human ATM kinase inhibition. Nat.Struct.Mol.Biol., 28:789-798, 2021 Cited by PubMed Abstract: 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 ATPγS and to the ATM inhibitors KU-55933 and M4076 at 2.8 Å, 2.8 Å and 3.0 Å 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. PubMed: 34556870DOI: 10.1038/s41594-021-00654-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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