4A1G
The crystal structure of the human Bub1 TPR domain in complex with the KI motif of Knl1
Summary for 4A1G
| Entry DOI | 10.2210/pdb4a1g/pdb |
| Descriptor | MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1, PROTEIN CASC5 (3 entities in total) |
| Functional Keywords | cell cycle, transferase, spindle assembly checkpoint, mitosis, tpr repeat, knl1, kmn network |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Nucleus: O43683 Q8NG31 |
| Total number of polymer chains | 8 |
| Total formula weight | 96132.22 |
| Authors | Krenn, V.,Wehenkel, A.,Li, X.,Santaguida, S.,Musacchio, A. (deposition date: 2011-09-15, release date: 2012-02-29, Last modification date: 2023-12-20) |
| Primary citation | Krenn, V.,Wehenkel, A.,Li, X.,Santaguida, S.,Musacchio, A. Structural Analysis Reveals Features of the Spindle Checkpoint Kinase Bub1-Kinetochore Subunit Knl1 Interaction. J.Cell Biol., 196:451-, 2012 Cited by PubMed Abstract: The function of the essential checkpoint kinases Bub1 and BubR1 requires their recruitment to mitotic kinetochores. Kinetochore recruitment of Bub1 and BubR1 is proposed to rely on the interaction of the tetratricopeptide repeats (TPRs) of Bub1 and BubR1 with two KI motifs in the outer kinetochore protein Knl1. We determined the crystal structure of the Bub1 TPRs in complex with the cognate Knl1 KI motif and compared it with the structure of the equivalent BubR1TPR-KI motif complex. The interaction developed along the convex surface of the TPR assembly. Point mutations on this surface impaired the interaction of Bub1 and BubR1 with Knl1 in vitro and in vivo but did not cause significant displacement of Bub1 and BubR1 from kinetochores. Conversely, a 62-residue segment of Bub1 that includes a binding domain for the checkpoint protein Bub3 and is C terminal to the TPRs was necessary and largely sufficient for kinetochore recruitment of Bub1. These results shed light on the determinants of kinetochore recruitment of Bub1. PubMed: 22331848DOI: 10.1083/JCB.201110013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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