1D9S
TUMOR SUPPRESSOR P15(INK4B) STRUCTURE BY COMPARATIVE MODELING AND NMR DATA
Summary for 1D9S
| Entry DOI | 10.2210/pdb1d9s/pdb |
| NMR Information | BMRB: 4701 |
| Descriptor | CYCLIN-DEPENDENT KINASE 4 INHIBITOR B (1 entity in total) |
| Functional Keywords | helix-turn-helix, ankyrin repeat, signaling protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 14355.20 |
| Authors | Yuan, C.,Ji, L.,Selby, T.L.,Byeon, I.J.L.,Tsai, M.D. (deposition date: 1999-10-29, release date: 2000-07-28, Last modification date: 2024-05-22) |
| Primary citation | Yuan, C.,Li, J.,Selby, T.L.,Byeon, I.J.,Tsai, M.D. Tumor suppressor INK4: comparisons of conformational properties between p16(INK4A) and p18(INK4C). J.Mol.Biol., 294:201-211, 1999 Cited by PubMed Abstract: The INK4 (inhibitor of cyclin-dependent kinase 4) family consists of four tumor-suppressor proteins: p15(INK4B), p16(INK4A), p18(INK4C), and p19(INK4D). While their sequences and structures are highly homologous, they show appreciable differences in conformational flexibility, stability, and aggregation tendency. Here, p16 and p18 were first compared directly by NMR for line broadening and disappearance, then investigated by three different approaches in search of the causes of these differences. From denaturation experiments it was found that both proteins are marginally stable with low denaturation stability (1.94 and 2.98 kcal/mol, respectively). Heteronuclear (1)H-(15)N nuclear Overhauser enhancement measurements revealed very limited conformational flexibility on the pico- to nanosecond time-scale for both p16 and p18. H/(2)H exchange of amide protons monitored by NMR on three proteins (p16, p18 as well as p15), however, revealed markedly different rates in the order p18 DOI: 10.1006/jmbi.1999.3231 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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