title: High-resolution structural characterization of a helical alpha/beta-peptide foldamer bound to the anti-apoptotic protein Bcl-xL.
abstract: Get into the groove: The first high-resolution structure of a foldamer bound to a protein target is described (see picture; foldamer in sticks). The foldamer consists of alpha- and beta-amino acid residues and is bound to the anti-apoptotic protein Bcl-x(L). The overall binding mode and key interactions observed in the foldamer/Bcl-x(L) complex mimic those seen in complexes of Bcl-x(L) with natural alpha-peptide ligands. Additional contacts in the foldamer/Bcl-x(L) complex involving beta-amino acid residues appear to contribute to binding affinity.
authors.affiliation: Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3052, Australia.
authors.forename: Erinna F
authors.initials: EF
authors.lastname: Lee
authors.forename: Jack D
authors.initials: JD
authors.lastname: Sadowsky
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Smith
authors.forename: Peter E
authors.initials: PE
authors.lastname: Czabotar
authors.forename: Kimberly J
authors.initials: KJ
authors.lastname: Peterson-Kaufman
authors.forename: Peter M
authors.initials: PM
authors.lastname: Colman
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
authors.forename: W Douglas
authors.initials: WD
authors.lastname: Fairlie
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D051020:bcl-X Protein / Q000737:chemistry*
chemical_list: D010455:Peptides; D051020:bcl-X Protein