2lny | pdb_00002lny

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

spinqualitylabelsall models 2lny, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lny is a 1 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.,Weingarth M, Ader C, Melquiond AJ, Nand D, Pongs O, Becker S, Bonvin AM, Baldus M Biophys J. 2012 Jul 3;103(1):29-37. PMID:22828329 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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