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

Naoya Tochio, Seizo Koshiba, Naohiro Kobayashi, Makoto Inoue, Takashi Yabuki, Masaaki Aoki, Eiko Seki, Takayoshi Matsuda, Yasuko Tomo, Yoko Motoda, Atsuo Kobayashi, Akiko Tanaka, Yoshihide Hayashizaki, Takaho Terada, Mikako Shirouzu, Takanori Kigawa, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)

Abstract

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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish
Pages (from-to)2534-2543
Number of pages10
JournalProtein Science
Volume15
Issue number11
DOIs
Publication statusPublished - 2006
Externally publishedYes

Keywords

  • C-TAK1
  • ELKL
  • KA1
  • MARK
  • Nuclear magnetic resonance
  • Solution structure

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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