Summary for 2XYN
| Entry DOI | 10.2210/pdb2xyn/pdb |
| Descriptor | TYROSINE-PROTEIN KINASE ABL2, SODIUM ION, CYCLOPROPANECARBOXYLIC ACID {4-[4-(4-METHYL-PIPERAZIN-1-YL)-6-(5-METHYL-2H-PYRAZOL-3-YLAMINO)-PYRIMIDIN-2-YLSULFANYL]-PHENYL}-AMIDE, ... (5 entities in total) |
| Functional Keywords | cell adhesion, structural genomics consortium, sgc, transferase |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 3 |
| Total formula weight | 103963.61 |
| Authors | Salah, E.,Ugochukwu, E.,Elkins, J.M.,Barr, A.J.,Shrestha, B.,Savitsky, P.,Mahajan, P.,Muniz, J.R.C.,Yue, W.W.,Chaikuad, A.,von Delft, F.,Bountra, C.,Arrowsmith, C.H.,Weigelt, J.,Edwards, A.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2010-11-18, release date: 2010-12-01, Last modification date: 2023-12-20) |
| Primary citation | Salah, E.,Ugochukwu, E.,Barr, A.J.,von Delft, F.,Knapp, S.,Elkins, J.M. Crystal Structures of Abl-Related Gene (Abl2) in Complex with Imatinib, Tozasertib (Vx-680), and a Type I Inhibitor of the Triazole Carbothioamide Class. J.Med.Chem., 54:2359-, 2011 Cited by PubMed Abstract: ABL2 (also known as ARG (ABL related gene)) is closely related to the well-studied Abelson kinase cABL. ABL2 is involved in human neoplastic diseases and is deregulated in solid tumors. Oncogenic gene translocations occur in acute leukemia. So far no structural information for ABL2 has been reported. To elucidate structural determinants for inhibitor interaction, we determined the cocrystal structure of ABL2 with the oncology drug imatinib. Interestingly, imatinib not only interacted with the ATP binding site of the inactive kinase but was also bound to the regulatory myristate binding site. This structure may therefore serve as a tool for the development of allosteric ABL inhibitors. In addition, we determined the structures of ABL2 in complex with VX-680 and with an ATP-mimetic type I inhibitor, which revealed an interesting position of the DFG motif intermediate between active and inactive conformations, that may also serve as a template for future inhibitor design. PubMed: 21417343DOI: 10.1021/JM101506N PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.81 Å) |
Structure validation
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