1UL7
Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3
Summary for 1UL7
| Entry DOI | 10.2210/pdb1ul7/pdb |
| NMR Information | BMRB: 10025 |
| Descriptor | MAP/microtubule affinity-regulating kinase 3 (1 entity in total) |
| Functional Keywords | ka1 domain, elkl motif, mark3, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transferase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 11533.26 |
| Authors | Tochio, N.,Koshiba, S.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-09-10, release date: 2004-03-10, Last modification date: 2023-12-27) |
| Primary citation | Tochio, N.,Koshiba, S.,Kobayashi, N.,Inoue, M.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Tomo, Y.,Motoda, Y.,Kobayashi, A.,Tanaka, A.,Hayashizaki, Y.,Terada, T.,Shirouzu, M.,Kigawa, T.,Yokoyama, S. Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3 Protein Sci., 15:2534-2543, 2006 Cited by PubMed 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 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. PubMed: 17075132DOI: 10.1110/ps.062391106 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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