Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain StructureReport as inadecuate




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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.



Author: Pan Li , Pan Shi , Chaohua Lai, Juan Li, Yuanyuan Zheng, Ying Xiong, Longhua Zhang , Changlin Tian

Source: http://plos.srce.hr/



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