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(1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a solub...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343089/ https://www.ncbi.nlm.nih.gov/pubmed/27981425 http://dx.doi.org/10.1007/s12104-016-9720-9 |
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author | Czarnota, Sylwia Baxter, Nicola J. Cliff, Matthew J. Waltho, Jonathan P. Scrutton, Nigel S. Hay, Sam |
author_facet | Czarnota, Sylwia Baxter, Nicola J. Cliff, Matthew J. Waltho, Jonathan P. Scrutton, Nigel S. Hay, Sam |
author_sort | Czarnota, Sylwia |
collection | PubMed |
description | Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT), found mostly in the brain. Here we report the backbone (1)H, (15)N and (13)C chemical shift assignments of S-COMT in complex with S-adenosyl-l-methionine, 3,5-dinitrocatechol and Mg(2+). Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97 % of all backbone resonances were assigned in the complex, with 205 out of a possible 215 residues assigned in the (1)H-(15)N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS+ webserver is in good agreement with published X-ray crystal structures. |
format | Online Article Text |
id | pubmed-5343089 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-53430892017-03-21 (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol Czarnota, Sylwia Baxter, Nicola J. Cliff, Matthew J. Waltho, Jonathan P. Scrutton, Nigel S. Hay, Sam Biomol NMR Assign Article Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT), found mostly in the brain. Here we report the backbone (1)H, (15)N and (13)C chemical shift assignments of S-COMT in complex with S-adenosyl-l-methionine, 3,5-dinitrocatechol and Mg(2+). Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97 % of all backbone resonances were assigned in the complex, with 205 out of a possible 215 residues assigned in the (1)H-(15)N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS+ webserver is in good agreement with published X-ray crystal structures. Springer Netherlands 2016-12-15 2017 /pmc/articles/PMC5343089/ /pubmed/27981425 http://dx.doi.org/10.1007/s12104-016-9720-9 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Article Czarnota, Sylwia Baxter, Nicola J. Cliff, Matthew J. Waltho, Jonathan P. Scrutton, Nigel S. Hay, Sam (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol |
title | (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol |
title_full | (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol |
title_fullStr | (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol |
title_full_unstemmed | (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol |
title_short | (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol |
title_sort | (1)h, (15)n, (13)c backbone resonance assignments of human soluble catechol o-methyltransferase in complex with s-adenosyl-l-methionine and 3,5-dinitrocatechol |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343089/ https://www.ncbi.nlm.nih.gov/pubmed/27981425 http://dx.doi.org/10.1007/s12104-016-9720-9 |
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