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Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure

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 cytoso...

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Autores principales: Li, Pan, Shi, Pan, Lai, Chaohua, Li, Juan, Zheng, Yuanyuan, Xiong, Ying, Zhang, Longhua, Tian, Changlin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4210162/
https://www.ncbi.nlm.nih.gov/pubmed/25347290
http://dx.doi.org/10.1371/journal.pone.0111035
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author Li, Pan
Shi, Pan
Lai, Chaohua
Li, Juan
Zheng, Yuanyuan
Xiong, Ying
Zhang, Longhua
Tian, Changlin
author_facet Li, Pan
Shi, Pan
Lai, Chaohua
Li, Juan
Zheng, Yuanyuan
Xiong, Ying
Zhang, Longhua
Tian, Changlin
author_sort Li, Pan
collection PubMed
description 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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spelling pubmed-42101622014-10-30 Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure Li, Pan Shi, Pan Lai, Chaohua Li, Juan Zheng, Yuanyuan Xiong, Ying Zhang, Longhua Tian, Changlin PLoS One Research Article 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. Public Library of Science 2014-10-27 /pmc/articles/PMC4210162/ /pubmed/25347290 http://dx.doi.org/10.1371/journal.pone.0111035 Text en © 2014 Li et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Li, Pan
Shi, Pan
Lai, Chaohua
Li, Juan
Zheng, Yuanyuan
Xiong, Ying
Zhang, Longhua
Tian, Changlin
Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
title Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
title_full Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
title_fullStr Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
title_full_unstemmed Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
title_short Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
title_sort solution nmr of mps-1 reveals a random coil cytosolic domain structure
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4210162/
https://www.ncbi.nlm.nih.gov/pubmed/25347290
http://dx.doi.org/10.1371/journal.pone.0111035
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