Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3
| Autor: | Akiko Tanaka, Makoto Inoue, Takayoshi Matsuda, Yoshihide Hayashizaki, Shigeyuki Yokoyama, Atsuo Kobayashi, Masaaki Aoki, Takashi Yabuki, Naohiro Kobayashi, Takanori Kigawa, Yasuko Tomo, Seizo Koshiba, Yoko Motoda, Eiko Seki, Mikako Shirouzu, Takaho Terada, Naoya Tochio |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein Folding EGF-like domain Molecular Sequence Data Protein domain Immunoglobulin domain Protein Serine-Threonine Kinases Biology Biochemistry Article SH3 domain HAMP domain Mice EVH1 domain Animals Amino Acid Sequence B3 domain Nuclear Magnetic Resonance Biomolecular Molecular Biology Binding Sites Sequence Homology Amino Acid Protein Structure Tertiary Structural Homology Protein Cyclic nucleotide-binding domain Solvents Biophysics Hydrophobic and Hydrophilic Interactions Microtubule-Associated Proteins Sequence Alignment |
| Zdroj: | Protein Science. 15:2534-2543 |
| ISSN: | 1469-896X 0961-8368 |
| Popis: | 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 approximately 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 betaalphabetabetabetabetaalpha 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. |
| Databáze: | OpenAIRE |
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