2oxk
From Proteopedia
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Helix Bundle Quaternary Structure from alpha/beta-Peptide Foldamers: GCN4-pLI with beta-residues at b and f heptad positions.
Overview
The function of a protein generally depends on adoption of a specific, folding pattern, which in turn is determined by the side chain sequence, along the polypeptide backbone. Here we show that the sequence-encoded, structural information in peptides derived from yeast transcriptional, activator GCN4 can be used to prepare hybrid alpha/beta-peptide foldamers, that adopt helix bundle quaternary structures. Crystal structures of two, hybrid alpha/beta-peptides are reported along with detailed structural, comparison to alpha-peptides of analogous side chain sequence. There is, considerable homology between alpha- and alpha/beta-peptides at the level, of helical secondary structure, with modest but significant differences in, the association geometry of helices in the quaternary structure.
About this Structure
2OXK is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Helix Bundle Quaternary Structure from alpha/beta-Peptide Foldamers., Horne WS, Price JL, Keck JL, Gellman SH, J Am Chem Soc. 2007 Apr 11;129(14):4178-80. Epub 2007 Mar 16. PMID:17362016
Page seeded by OCA on Tue Jan 29 21:17:27 2008
Categories: Protein complex | Gellman, S.H. | Horne, W.S. | Keck, J.L. | Price, J.L. | FMT | Coiled coil | Foldamer | Helix bundle
