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

Summary for 3F86

Entry DOI	10.2210/pdb3f86/pdb
Related	1GCL 2OXJ 2OXK 2ZTA
Descriptor	GCN4pLI-betaAD (2 entities in total)
Functional Keywords	alpha/beta-peptide, helix bundle, foldamer, coiled coil, gcn4 derivative, unknown function
Total number of polymer chains	8
Total formula weight	33696.79
Authors	Giuliano, M.W.,Horne, W.S.,Gellman, S.H. (deposition date: 2008-11-11, release date: 2009-07-21, Last modification date: 2023-11-15)
Primary citation	Giuliano, M.W.,Horne, W.S.,Gellman, S.H. An alpha/beta-peptide helix bundle with a pure beta3-amino acid core and a distinctive quaternary structure. J.Am.Chem.Soc., 131:9860-9861, 2009 Cited by PubMed Abstract: 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. PubMed: 19580264 DOI: 10.1021/ja8099294 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation