التفاصيل البيبلوغرافية
| العنوان: |
Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure. |
| المؤلفون: |
Li, Pan1, Shi, Pan2, Lai, Chaohua1, Li, Juan1, Zheng, Yuanyuan1 zlhustc@ustc.edu.cn, Xiong, Ying1, Zhang, Longhua1, Tian, Changlin1,2 cltian@ustc.edu.cn |
| المصدر: |
PLoS ONE. Oct2014, Vol. 9 Issue 10, p1-7. 7p. |
| مصطلحات موضوعية: |
*MAGNETIC domain, *FERROMAGNETIC materials, *MAGNETIC properties of condensed matter, *CAENORHABDITIS elegans, *NEMATODES |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
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