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Protein Science (2006), 15:2534-2543. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3

Naoya Tochio1,4, Seizo Koshiba1,4, Naohiro Kobayashi1, Makoto Inoue1, Takashi Yabuki1, Masaaki Aoki1, Eiko Seki1, Takayoshi Matsuda1, Yasuko Tomo1, Yoko Motoda1, Atsuo Kobayashi1, Akiko Tanaka1, Yoshihide Hayashizaki1, Takaho Terada1, Mikako Shirouzu1, Takanori Kigawa1,2, and Shigeyuki Yokoyama1,3

1 RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan
2 Department of Computational Intelligence and Systems Science, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, Midori, Yokohama 226-8502, Japan
3 Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan

(RECEIVED June 8, 2006; FINAL REVISION August 15, 2006; ACCEPTED August 16, 2006)

Microtubule-associated protein/microtubule affinity-regulating kinases (MARKs)/PAR-1 are common regulators of cell polarity that are conserved from nematode to human. All of these kinases have a highly conserved C-terminal domain, which is termed the kinase-associated domain 1 (KA1), although its function is unknown. In this study, we determined the solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy. We found that ~50 additional residues preceding the previously defined KA1 domain are required for its proper folding. The newly defined KA1 domain adopts a compact {alpha}+beta structure with a beta{alpha}betabetabetabeta{alpha} topology. We also found a characteristic hydrophobic, concave surface surrounded by positively charged residues. This concave surface includes the highly conserved Glu-Leu-Lys-Leu motif at the C terminus, indicating that it is important for the function of the KA1 domain.

Keywords: MARK; C-TAK1; KA1; ELKL; nuclear magnetic resonance; solution structure


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