3FDM

alpha/beta foldamer in complex with Bcl-xL

Summary for 3FDM

• Entry DOI: 10.2210/pdb3fdm/pdb
• Related: 3FDL
• Descriptor: Apoptosis regulator Bcl-X, alpha/beta-peptide foldamer, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: protein-peptide complex, helical bundle, foldamer, apoptosis, alternative splicing, membrane, mitochondrion, nucleus, transmembrane
• Biological source: Homo sapiens (Human); More
• Cellular location: Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817
• Total number of polymer chains: 6
• Total formula weight: 59677.92

Authors

Fairlie, W.D.,Lee, E.F.,Smith, B.J.,Czabotar, P.E.,Colman, P.M.,Sadowsky, J.D.,Peterson-Kaufman, K.J.,Gellman, S.H. (deposition date: 2008-11-26, release date: 2009-03-10, Last modification date: 2023-11-15)

Primary citation

Lee, E.F.,Sadowsky, J.D.,Smith, B.J.,Czabotar, P.E.,Peterson-Kaufman, K.J.,Colman, P.M.,Gellman, S.H.,Fairlie, W.D.
High-Resolution Structural Characterization of a Helical alpha/beta-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-x(L)
Angew.Chem.Int.Ed.Engl., 48:4318-4322, 2009

PubMed 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.

PubMed: 19229915
DOI: 10.1002/anie.200805761

Experimental method

X-RAY DIFFRACTION (2.26 Å)