1MUO
CRYSTAL STRUCTURE OF AURORA-2, AN ONCOGENIC SERINE-THREONINE KINASE
Summary for 1MUO
| Entry DOI | 10.2210/pdb1muo/pdb |
| Descriptor | Aurora-related kinase 1, ADENOSINE (2 entities in total) |
| Functional Keywords | transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytoskeleton, centrosome: O14965 |
| Total number of polymer chains | 1 |
| Total formula weight | 34699.48 |
| Authors | Cheetham, G.M.T.,Knegtel, R.M.A.,Coll, J.T.,Renwick, S.B.,Swenson, L.,Weber, P.,Lippke, J.A.,Austen, D.A. (deposition date: 2002-09-24, release date: 2003-04-15, Last modification date: 2024-02-14) |
| Primary citation | Cheetham, G.M.T.,Knegtel, R.M.A.,Coll, J.T.,Renwick, S.B.,Swenson, L.,Weber, P.,Lippke, J.A.,Austen, D.A. Crystal Structure of Aurora-2, an Oncogenic Serine/Threonine Kinase J.Biol.Chem., 277:42419-42422, 2002 Cited by PubMed Abstract: Aurora-2 is a key member of a closely related subgroup of serine/threonine kinases that plays important roles in the completion of essential mitotic events. Aurora-2 is oncogenic and amplified in various human cancers and could be an important therapeutic target for inhibitory molecules that would disrupt the cell cycle and block proliferation. We report the first crystal structure of Aurora-2 kinase in complex with adenosine. Analysis of residues in the active site suggests differences with structurally and biologically related protein kinases. The activation loop, which contains residues specific to the Aurora family of kinases, has a unique conformation. These results provide valuable insight into the design of selective and highly potent ATP-competitive inhibitors of the Aurora kinases. PubMed: 12237287DOI: 10.1074/jbc.C200426200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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