1BLX
P19INK4D/CDK6 COMPLEX
Summary for 1BLX
Entry DOI | 10.2210/pdb1blx/pdb |
Descriptor | CYCLIN-DEPENDENT KINASE 6, P19INK4D, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | inhibitor protein, cyclin-dependent kinase, cell cycle control, alpha/beta, complex (inhibitor protein-kinase), complex (inhibitor protein-kinase) complex, complex (inhibitor protein/kinase) |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 54859.78 |
Authors | Brotherton, D.H.,Dhanaraj, V.,Wick, S.,Brizuela, L.,Domaille, P.J.,Volyanik, E.,Xu, X.,Parisini, E.,Smith, B.O.,Archer, S.J.,Serrano, M.,Brenner, S.L.,Blundell, T.L.,Laue, E.D. (deposition date: 1998-07-21, release date: 1999-06-01, Last modification date: 2024-05-22) |
Primary citation | Brotherton, D.H.,Dhanaraj, V.,Wick, S.,Brizuela, L.,Domaille, P.J.,Volyanik, E.,Xu, X.,Parisini, E.,Smith, B.O.,Archer, S.J.,Serrano, M.,Brenner, S.L.,Blundell, T.L.,Laue, E.D. Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d. Nature, 395:244-250, 1998 Cited by PubMed Abstract: The crystal structure of the cyclin D-dependent kinase Cdk6 bound to the p19 INK4d protein has been determined at 1.9 A resolution. The results provide the first structural information for a cyclin D-dependent protein kinase and show how the INK4 family of CDK inhibitors bind. The structure indicates that the conformational changes induced by p19INK4d inhibit both productive binding of ATP and the cyclin-induced rearrangement of the kinase from an inactive to an active conformation. The structure also shows how binding of an INK4 inhibitor would prevent binding of p27Kip1, resulting in its redistribution to other CDKs. Identification of the critical residues involved in the interaction explains how mutations in Cdk4 and p16INK4a result in loss of kinase inhibition and cancer. PubMed: 9751051DOI: 10.1038/26164 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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