2LNY

ShB peptide structure bound to negatively charged lipid-bilayer after Molecular Dynamics refinement

Summary for 2LNY

• Entry DOI: 10.2210/pdb2lny/pdb
• NMR Information: BMRB: 18184
• Descriptor: ShB peptide (1 entity in total)
• Functional Keywords: de novo-peptide, n-type inactivation, potassium channel, de novo protein
• Biological source: artificial gene
• Total number of polymer chains: 1
• Total formula weight: 2233.57

Authors

Weingarth, M. (deposition date: 2012-01-06, release date: 2012-08-08, Last modification date: 2024-05-15)

Primary citation

Weingarth, M.,Ader, C.,Melquiond, A.J.,Nand, D.,Pongs, O.,Becker, S.,Bonvin, A.M.,Baldus, M.
Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.
Biophys.J., 103:29-37, 2012

PubMed Abstract: Elemental biological functions such as molecular signal transduction are determined by the dynamic interplay between polypeptides and the membrane environment. Determining such supramolecular arrangements poses a significant challenge for classical structural biology methods. We introduce an iterative approach that combines magic-angle spinning solid-state NMR spectroscopy and atomistic molecular dynamics simulations for the determination of the structure and topology of membrane-bound systems with a resolution and level of accuracy difficult to obtain by either method alone. Our study focuses on the Shaker B ball peptide that is representative for rapid N-type inactivating domains of voltage-gated K(+) channels, associated with negatively charged lipid bilayers.

PubMed: 22828329
DOI: 10.1016/j.bpj.2012.05.016

Experimental method

SOLID-STATE NMR