| Literature DB >> 8564545 |
K Ogata1, C Kanei-Ishii, M Sasaki, H Hatanaka, A Nagadoi, M Enari, H Nakamura, Y Nishimura, S Ishii, A Sarai.
Abstract
The DNA-binding domain of Myb consists of three imperfect repeats, R1, R2 and R3, each containing a helix-turn-helix motif variation. Among these repeats, R2 has distinct characteristics with high thermal instability. The NMR structure analysis found a cavity inside the hydrophobic core of R2 but not in R1 or R3. Here, we show that R2 has slow conformational fluctuations, and that a cavity-filling mutation which stabilizes the R2 structure significantly reduces specific Myb DNA-binding activity and trans-activation. Structural observations of the free and DNA-complexed stages suggest that the implied inherent conformational flexibility of R2, associated with the presence of the cavity, could be important for DNA recognition by Myb.Entities:
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Year: 1996 PMID： 8564545 DOI： 10.1038/nsb0296-178
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368