1lcm
From Proteopedia
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MICROCYSTIN-LR, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
NMR spectroscopy in aqueous and dimethyl sulfoxide/water solutions is used, to determine the three-dimensional structures of microcystin-LR, a cyclic, cyanobacterial heptapeptide toxin which is a potent inhibitor of type 1, and type 2A protein phosphatases. The conformations of this toxic peptide, are studied using a simulated annealing (SA) protocol followed by refined, SA calculations in vacuo and free MD simulations in water. Only one, conformational family in each solvent is found. The peptide ring has a, saddle-shaped form, essentially the same in both solvents. The structural, difference observed between the two solution structures is located to the, part consisting of Mdha, Ala, and Leu. This peptide segment is not present, in nodularin, a cyclic pentapeptide of similar toxicity. The Arg side, chain is very flexible, while the side chain of Leu is well defined. The, side chain of Adda, essential for toxicity, is constrained in the vicinity, of the backbone ring but appears to be flexible in the more remote part.
About this Structure
1LCM is a Protein complex structure of sequences from Microcystis aeruginosa. Full crystallographic information is available from OCA.
Reference
Conformational studies of microcystin-LR using NMR spectroscopy and molecular dynamics calculations., Trogen GB, Annila A, Eriksson J, Kontteli M, Meriluoto J, Sethson I, Zdunek J, Edlund U, Biochemistry. 1996 Mar 12;35(10):3197-205. PMID:8605154
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