6GVJ
Human Mps1 kinase domain with ordered activation loop
Summary for 6GVJ
| Entry DOI | 10.2210/pdb6gvj/pdb |
| Descriptor | Dual specificity protein kinase TTK, GLYCEROL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | mps1, ttk, kinase, mitosis checkpoint, transferase, activation loop, activation segment |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 49496.04 |
| Authors | Roorda, J.C.,Hiruma, Y.,Joosten, R.P.,Perrakis, A. (deposition date: 2018-06-21, release date: 2019-01-09, Last modification date: 2024-01-17) |
| Primary citation | Roorda, J.C.,Joosten, R.P.,Perrakis, A.,Hiruma, Y. A crystal structure of the human protein kinase Mps1 reveals an ordered conformation of the activation loop. Proteins, 87:348-352, 2019 Cited by PubMed Abstract: Monopolar spindle 1 (Mps1) is a dual-specificity protein kinase, orchestrating faithful chromosome segregation during mitosis. All reported structures of the Mps1 kinase adopt the hallmarks of an inactive conformation, which includes a mostly disordered activation loop. Here, we present a 2.4 Å resolution crystal structure of an "extended" version of the Mps1 kinase domain, which shows an ordered activation loop. However, the other structural characteristics of an active kinase are not present. Our structure shows that the Mps1 activation loop can fit to the ATP binding pocket and interferes with ATP, but less so with inhibitors binding, partly explain the potency of various Mps1 inhibitors. PubMed: 30582207DOI: 10.1002/prot.25651 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.41 Å) |
Structure validation
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