3A7F
Human MST3 kinase
Summary for 3A7F
| Entry DOI | 10.2210/pdb3a7f/pdb |
| Related | 3A7G 3A7H 3A7I 3A7J |
| Descriptor | Serine/threonine kinase 24 (STE20 homolog, yeast) (2 entities in total) |
| Functional Keywords | two-lobe protein kinase fold, atp-binding, kinase, nucleotide-binding, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34336.19 |
| Authors | Ko, T.P.,Jeng, W.Y.,Liu, C.I.,Lai, M.D.,Wang, A.H.J. (deposition date: 2009-09-26, release date: 2010-02-02, Last modification date: 2024-10-16) |
| Primary citation | Ko, T.P.,Jeng, W.Y.,Liu, C.I.,Lai, M.D.,Wu, C.L.,Chang, W.J.,Shr, H.L.,Lu, T.J.,Wang, A.H.J. Structures of human MST3 kinase in complex with adenine, ADP and Mn2+. Acta Crystallogr.,Sect.D, 66:145-154, 2010 Cited by PubMed Abstract: The MST family is a subclass of mammalian serine/threonine kinases that are related to the yeast sterile-20 protein and are implicated in regulating cell growth and transformation. The MST3 protein contains a 300-residue catalytic domain and a 130-residue regulatory domain, which can be cleaved by caspase and activated by autophosphorylation, promoting apoptosis. Here, five crystal structures of the catalytic domain of MST3 are presented, including a complex with ADP and manganese, a unique cofactor preferred by the enzyme, and a complex with adenine. Similar to other protein kinases, the catalytic domain of MST3 folds into two lobes: the smaller N lobe forms the nucleotide-binding site and the larger C lobe recognizes the polypeptide substrate. The bound ADP and Mn(2+) ions are covered by a glycine-rich loop and held in place by Asn149 and Asp162. A different orientation was observed for the ligand in the MST3-adenine complex. In the activation loop, the side chain of Thr178 is phosphorylated and is sandwiched by Arg143 and Arg176. Comparison of this structure with other similar kinase structures shows a 180 degrees rotation of the loop, leading to activation of the enzyme. The well defined protein-ligand interactions also provide useful information for the design of potent inhibitors. PubMed: 20124694DOI: 10.1107/S0907444909047507 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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