3f86

An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quaternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions

spinqualitylabelsall models 3f86, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3f86 is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ACE, B3L, B3M, BIL, HMR Related: 2oxk, 2oxj, 1gcl, 2zta Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Helix bundles are among the most widely studied tertiary and quaternary structural motifs in proteins. Here we present the crystal structure of an alpha/beta-peptide foldamer that adopts a tetrameric helix-bundle quaternary structure with a hydrophobic core composed solely of beta-amino acids. The structure displays features that are unprecedented among all known helix bundles composed of either alpha-peptides or peptidic foldamers. The tetramer is characterized by an asymmetry of interaction between neighboring helices, and the side-chain packing within the hydrophobic core differs fundamentally from the knobs-into-holes arrangement typical of most helix bundles. An alpha/beta-Peptide Helix Bundle with a Pure beta(3)-Amino Acid Core and a Distinctive Quaternary Structure.,Giuliano MW, Horne WS, Gellman SH J Am Chem Soc. 2009 Jul 6. PMID:19580264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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