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Comparison of the free and DNA-complexed forms of the DMA-binding domain from c-Myb

Nature Structural Biology volume 2, pages 309–320 (1995)Cite this article

Abstract

The DNA-binding domain of c-Myb consists of three imperfect tandem repeats (R1, R2 and R3). The three repeats have similar overall architectures, each containing a helix-turn-helix variation motif. The three conserved tryptophans in each repeat participate in forming a hydrophobic core. Comparison of the three repeat structures indicated that cavities are found in the hydrophobic core of R2, which is thermally unstable. On complexation with DNA, the orientations of R2 and R3 are fixed by tight binding and their conformations are slightly changed. No significant changes occur in the chemical shifts of R1 consistent with its loose interaction with DNA.

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Authors and Affiliations

  1. Graduate School of Integrated Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama, 236, Japan

    Kazuhiro Ogata, Yuko Ametani, Zenzo Hirata & Yoshifumi Nishimura

  2. Protein Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka, 565, Japan

    Souichi Morikawa & Haruki Nakamura

  3. Protein Research Institute, Osaka University, 3-21 Yamada-oka, Osaka, 565, Japan

    Hironobu Hojo, Shoko Yoshimura, Ruoheng Zhang & Saburo Aimoto

  4. Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki, 305, Japan

    Kazuhiro Ogata, Akinori Sarai & Shunsuke Ishii

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Ogata, K., Morikawa, S., Nakamura, H. et al. Comparison of the free and DNA-complexed forms of the DMA-binding domain from c-Myb. Nat Struct Mol Biol 2, 309–320 (1995). https://doi.org/10.1038/nsb0495-309

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