Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure |
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| Authors: | Pan Li Pan Shi Chaohua Lai Juan Li Yuanyuan Zheng Ying Xiong Longhua Zhang Changlin Tian |
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| Institution: | 1. Hefei National Laboratory of Microscale Physical Sciences, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, P. R. China.; 2. High Magnetic Field Laboratory, Hefei institutes of Physical Science, Chinese Academy of Sciences, Hefei, Anhui, P. R. China.; George Washington University, United States of America, |
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| Abstract: | Caenorhabditis elegans MPS1 is a single transmembrane helical auxiliary subunit that co-localizes with the voltage-gated potassium channel KVS1 in the nematode nervous system. MPS-1 shares high homology with KCNE (potassium voltage-gated channel subfamily E member) auxiliary subunits, and its cytosolic domain was reported to have a serine/threonine kinase activity that modulates KVS1 channel function via phosphorylation. In this study, NMR spectroscopy indicated that the full length and truncated MPS-1 cytosolic domain (134–256) in the presence or absence of n-dodecylphosphocholine detergent micelles adopted a highly flexible random coil secondary structure. In contrast, protein kinases usually adopt a stable folded conformation in order to implement substrate recognition and phosphoryl transfer. The highly flexible random coil secondary structure suggests that MPS-1 in the free state is unstructured but may require a substrate or binding partner to adopt stable structure required for serine/threonine kinase activity. |
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