Solution structure of nodularin

An inhibitor of serine/threonine-specific protein phosphatases

Arto Annila (Corresponding Author), J. Lehtimäki, Katri Mattila, J. Eriksson, K. Sivonen, T. Rantala, Torbjörn Drakenberg

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The three-dimensional solution structure of nodularin was studied by NMR and molecular dynamics simulations. The conformation in water was determined from the distance and dihedral data by distance geometry and refined by iterative relaxation matrix analysis. The cyclic backbone adopts a well defined conformation but the remote parts of the side chains of arginine as well as the amino acid derivative Adda have a large spatial dispersion. For the unusual amino acids the partial charges were calculated and nodularin was subjected to molecular dynamic simulations in water. A good agreement was found between experimental and computational data with hydrogen bonds, solvent accessibility, molecular motion, and conformational exchange. The three-dimensional structure resembles very closely that of microcystin-LR in the chemically equivalent segment. Therefore, it is expected that the binding of both microcystins and nodularins to serine/threonine-specific protein phosphatases is similar on an atomic level.
Original languageEnglish
Pages (from-to)16695-16702
Number of pages8
JournalJournal of Biological Chemistry
Volume271
DOIs
Publication statusPublished - 1996
MoE publication typeA1 Journal article-refereed

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Phosphoprotein Phosphatases
Threonine
Serine
Molecular Dynamics Simulation
Conformations
Molecular dynamics
Microcystins
Amino Acids
Water
Computer simulation
Arginine
Hydrogen
Hydrogen bonds
Nuclear magnetic resonance
Derivatives
Geometry
nodularin

Cite this

Annila, A., Lehtimäki, J., Mattila, K., Eriksson, J., Sivonen, K., Rantala, T., & Drakenberg, T. (1996). Solution structure of nodularin: An inhibitor of serine/threonine-specific protein phosphatases. Journal of Biological Chemistry, 271, 16695-16702. https://doi.org/10.1074/jbc.271.28.16695
Annila, Arto ; Lehtimäki, J. ; Mattila, Katri ; Eriksson, J. ; Sivonen, K. ; Rantala, T. ; Drakenberg, Torbjörn. / Solution structure of nodularin : An inhibitor of serine/threonine-specific protein phosphatases. In: Journal of Biological Chemistry. 1996 ; Vol. 271. pp. 16695-16702.
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abstract = "The three-dimensional solution structure of nodularin was studied by NMR and molecular dynamics simulations. The conformation in water was determined from the distance and dihedral data by distance geometry and refined by iterative relaxation matrix analysis. The cyclic backbone adopts a well defined conformation but the remote parts of the side chains of arginine as well as the amino acid derivative Adda have a large spatial dispersion. For the unusual amino acids the partial charges were calculated and nodularin was subjected to molecular dynamic simulations in water. A good agreement was found between experimental and computational data with hydrogen bonds, solvent accessibility, molecular motion, and conformational exchange. The three-dimensional structure resembles very closely that of microcystin-LR in the chemically equivalent segment. Therefore, it is expected that the binding of both microcystins and nodularins to serine/threonine-specific protein phosphatases is similar on an atomic level.",
author = "Arto Annila and J. Lehtim{\"a}ki and Katri Mattila and J. Eriksson and K. Sivonen and T. Rantala and Torbj{\"o}rn Drakenberg",
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Annila, A, Lehtimäki, J, Mattila, K, Eriksson, J, Sivonen, K, Rantala, T & Drakenberg, T 1996, 'Solution structure of nodularin: An inhibitor of serine/threonine-specific protein phosphatases', Journal of Biological Chemistry, vol. 271, pp. 16695-16702. https://doi.org/10.1074/jbc.271.28.16695

Solution structure of nodularin : An inhibitor of serine/threonine-specific protein phosphatases. / Annila, Arto (Corresponding Author); Lehtimäki, J.; Mattila, Katri; Eriksson, J.; Sivonen, K.; Rantala, T.; Drakenberg, Torbjörn.

In: Journal of Biological Chemistry, Vol. 271, 1996, p. 16695-16702.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Solution structure of nodularin

T2 - An inhibitor of serine/threonine-specific protein phosphatases

AU - Annila, Arto

AU - Lehtimäki, J.

AU - Mattila, Katri

AU - Eriksson, J.

AU - Sivonen, K.

AU - Rantala, T.

AU - Drakenberg, Torbjörn

PY - 1996

Y1 - 1996

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AB - The three-dimensional solution structure of nodularin was studied by NMR and molecular dynamics simulations. The conformation in water was determined from the distance and dihedral data by distance geometry and refined by iterative relaxation matrix analysis. The cyclic backbone adopts a well defined conformation but the remote parts of the side chains of arginine as well as the amino acid derivative Adda have a large spatial dispersion. For the unusual amino acids the partial charges were calculated and nodularin was subjected to molecular dynamic simulations in water. A good agreement was found between experimental and computational data with hydrogen bonds, solvent accessibility, molecular motion, and conformational exchange. The three-dimensional structure resembles very closely that of microcystin-LR in the chemically equivalent segment. Therefore, it is expected that the binding of both microcystins and nodularins to serine/threonine-specific protein phosphatases is similar on an atomic level.

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