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Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3
Author(s) -
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
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062391106
Subject(s) - microtubule , protein kinase domain , kinase , biology , microbiology and biotechnology , folding (dsp implementation) , protein structure , protein domain , conserved sequence , biochemistry , biophysics , peptide sequence , gene , engineering , mutant , electrical engineering
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.