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1ay3
From Proteopedia
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NODULARIN FROM NODULARIA SPUMIGENA
Overview
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.
About this Structure
1AY3 is a Protein complex structure of sequences from Nodularia spumigena with MFD as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of nodularin. An inhibitor of serine/threonine-specific protein phosphatases., Annila A, Lehtimaki J, Mattila K, Eriksson JE, Sivonen K, Rantala TT, Drakenberg T, J Biol Chem. 1996 Jul 12;271(28):16695-702. PMID:8663277
Page seeded by OCA on Sat Nov 24 23:29:49 2007
