4B94
Crystal structure of human Mps1 TPR domain
Summary for 4B94
| Entry DOI | 10.2210/pdb4b94/pdb |
| Related | 2X9E |
| Descriptor | DUAL SPECIFICITY PROTEIN KINASE TTK, TETRAETHYLENE GLYCOL, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | transferase, kinetochore, mitosis |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 4 |
| Total formula weight | 83192.49 |
| Authors | Littler, D.,von Castelmur, E.,De Marco, V.,Perrakis, A. (deposition date: 2012-08-31, release date: 2013-04-24, Last modification date: 2024-05-08) |
| Primary citation | Nijenhuis, W.,von Castelmur, E.,Littler, D.,De Marco, V.,Tromer, E.,Vleugel, M.,van Osch, M.H.,Snel, B.,Perrakis, A.,Kops, G.J. A Tpr Domain-Containing N-Terminal Module of Mps1 is Required for its Kinetochore Localization by Aurora B. J.Cell Biol., 201:217-, 2013 Cited by PubMed Abstract: The mitotic checkpoint ensures correct chromosome segregation by delaying cell cycle progression until all kinetochores have attached to the mitotic spindle. In this paper, we show that the mitotic checkpoint kinase MPS1 contains an N-terminal localization module, organized in an N-terminal extension (NTE) and a tetratricopeptide repeat (TPR) domain, for which we have determined the crystal structure. Although the module was necessary for kinetochore localization of MPS1 and essential for the mitotic checkpoint, the predominant kinetochore binding activity resided within the NTE. MPS1 localization further required HEC1 and Aurora B activity. We show that MPS1 localization to kinetochores depended on the calponin homology domain of HEC1 but not on Aurora B-dependent phosphorylation of the HEC1 tail. Rather, the TPR domain was the critical mediator of Aurora B control over MPS1 localization, as its deletion rendered MPS1 localization insensitive to Aurora B inhibition. These data are consistent with a model in which Aurora B activity relieves a TPR-dependent inhibitory constraint on MPS1 localization. PubMed: 23569217DOI: 10.1083/JCB.201210033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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