1DAY
CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-GMPPNP
Summary for 1DAY
| Entry DOI | 10.2210/pdb1day/pdb |
| Related | 1A6O 1DAW |
| Descriptor | PROTEIN KINASE CK2, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | protein kinase ck2, dual-cosubstrate specificity, binary complex with mg-gmppnp, transferase |
| Biological source | Zea mays |
| Total number of polymer chains | 1 |
| Total formula weight | 39244.20 |
| Authors | Niefind, K.,Puetter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D. (deposition date: 1999-11-01, release date: 2000-05-03, Last modification date: 2023-08-09) |
| Primary citation | Niefind, K.,Putter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D. GTP plus water mimic ATP in the active site of protein kinase CK2. Nat.Struct.Biol., 6:1100-1103, 1999 Cited by PubMed Abstract: The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property. PubMed: 10581548DOI: 10.1038/70033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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