4CEG
Crystal structure of Aurora A 122-403 C290A, C393A bound to ADP
Summary for 4CEG
| Entry DOI | 10.2210/pdb4ceg/pdb |
| Descriptor | AURORA KINASE A, ADENOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | transferase, protein kinase, mitosis |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 33766.45 |
| Authors | Burgess, S.G.,Bayliss, R. (deposition date: 2013-11-11, release date: 2015-01-28, Last modification date: 2024-11-06) |
| Primary citation | Burgess, S.G.,Bayliss, R. The Structure of C290A:C393A Aurora a Provides Structural Insights Into Kinase Regulation. Acta Crystallogr.,Sect.F, 71:315-, 2015 Cited by PubMed Abstract: Aurora A is a Ser/Thr protein kinase that functions in cell-cycle regulation and is implicated in cancer development. During mitosis, Aurora A is activated by autophosphorylation on its activation loop at Thr288. The Aurora A catalytic domain (amino acids 122-403) expressed in Escherichia coli autophosphorylates on two activation-loop threonine residues (Thr288 and Thr287), whereas a C290A,C393A double point mutant of the Aurora A catalytic domain autophosphorylates only on Thr288. The structure of the complex of this mutant with ADP and magnesium was determined to 2.1 Å resolution using molecular replacement. This is an improvement on the existing 2.75 Å resolution structure of the equivalent wild-type complex. The structure confirms that single phosphorylation of the activation loop on Thr288 is insufficient to stabilize a `fully active' conformation of the activation loop in the absence of binding to TPX2. PubMed: 25760707DOI: 10.1107/S2053230X15002290 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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