Solution structure of nodularin. An inhibitor of serine/threonine-specific protein phosphatases

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: Annila, Lehtimäki, Mattila, Eriksson, Sivonen, Rantala, Drakenberg
Publication year: 1996
Journal: Journal of Biological Chemistry
Journal acronym: J Biol Chem
Volume number: 271
Issue number: 28
Start page: 16695
End page: 16702
ISSN: 0021-9258
eISSN: 1083-351X


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.

Last updated on 2020-05-06 at 05:29