Thomas L. Selby

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to a variety of cellular proteins such as NF-␬B and I␬B (Hirai et al., 1994; Suzuki et al., 1996). Figure 1 shows the primary sequence of p16, along with that of other proteins in the p16 family: p15, p18, and p19, both human and murine. P16 is comprised mainly of four ankyrin repeats, a structural motif about Campus Chemical Instrument Center 33 amino(More)
Within the tumor suppressor protein INK4 ~inhibitor of cyclin-dependent kinase 4! family, p15 INK4B is the smallest and the only one whose structure has not been determined previously, probably due to the protein's conformational flexibility and instability. In this work, multidimensional NMR studies were performed on this protein. The first tertiary(More)
Since the structures of several ankyrin-repeat proteins including the INK4 (inhibitor of cyclin-dependent kinase 4) family have been reported recently, the detailed structures and the functional roles of the loops have drawn considerable interest. This paper addresses the potential importance of the loops of ankyrin-repeat proteins in three aspects. First,(More)
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(More)
We report the first detailed structure-function analyses of p18INK4C (p18), which is a homologue of the important tumor suppressor p16INK4A (p16). Twenty-four mutants were designed rationally. The global conformations of the mutants were characterized by NMR, while the function was assayed by inhibition of cyclin-dependent kinase 4 (CDK4). Most of these(More)
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