Towards understanding secondary structure transitions: phosphorylation and metal coordination in model peptides.

Article Details

Citation

Broncel M, Wagner SC, Paul K, Hackenberger CP, Koksch B

Towards understanding secondary structure transitions: phosphorylation and metal coordination in model peptides.

Org Biomol Chem. 2010 Jun 7;8(11):2575-9. doi: 10.1039/c001458c. Epub 2010 Mar 29.

PubMed ID
20485793 [ View in PubMed
]
Abstract

Secondary structure transitions are important modulators of signal transduction and protein aggregation. Phosphorylation is a well known post-translational modification capable of dramatic alteration of protein secondary structure. Additionally, phosphorylated residues can induce structural changes through metal binding. Data derived from the Protein Data Bank demonstrate that magnesium and manganese are metal ions most favored by phosphate. Due to the complexity of molecular interactions as well as the challenging physicochemical properties of natural systems, simplified peptide models have emerged as a useful tool for investigating the molecular switching phenomenon. In this study using a coiled coil model peptide, we show structural consequences of phosphorylation and subsequent magnesium and manganese ions coordination. In the course of our experiment we obtained a switch cascade starting from a stable helical conformation of the control peptide, continuing through the phosphorylation-induced unfolded structure, and ending with a metal-stabilized alpha-helix (Mg(2+)) or helical fibers (Mn(2+)), each of which could be transferred back to the unfolded form upon EDTA chelation. This study demonstrates how small peptide models can aid in the evaluation and a better understanding of protein secondary structure transitions.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Edetate calcium disodium anhydrousManganese cationSmall moleculeHumans
Yes
Chelator
Details
Edetate disodium anhydrousManganese cationSmall moleculeHumans
Unknown
Chelator
Details
Edetic acidManganese cationSmall moleculeHumans
Unknown
Chelator
Details