Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3

• Published in: Protein science Vol. 15; no. 11; pp. 2534 - 2543
• Main Authors: Tochio, Naoya, Koshiba, Seizo, Kobayashi, Naohiro, Inoue, Makoto, Yabuki, Takashi, Aoki, Masaaki, Seki, Eiko, Matsuda, Takayoshi, Tomo, Yasuko, Motoda, Yoko, Kobayashi, Atsuo, Tanaka, Akiko, Hayashizaki, Yoshihide, Terada, Takaho, Shirouzu, Mikako, Kigawa, Takanori, Yokoyama, Shigeyuki
• Format: Journal Article
• Language: English
• Published: Bristol Cold Spring Harbor Laboratory Press 01.11.2006; Blackwell Publishing
• Subjects: Amino Acid Sequence; Animals; Binding Sites; C‐TAK1; ELKL; Hydrophobic and Hydrophilic Interactions; KA1; MARK; Mice; Microtubule-Associated Proteins - chemistry; Models, Molecular; Molecular Sequence Data; nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular - methods; Protein Folding; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases - chemistry; Sequence Alignment - methods; Sequence Homology, Amino Acid; solution structure; Solvents; Structural Homology, Protein
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1110/ps.062391106

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 α+β structure with a βαββββα 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.