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BIBTEX RIS

High‐Resolution Structural Characterization of a Helical α/β‐Peptide Foldamer Bound to the Anti‐Apoptotic Protein Bcl‐x L

2009; Wiley; Volume: 48; Issue: 24 Linguagem: Inglês

10.1002/anie.200805761

ISSN

1521-3773

Autores

Erinna F. Lee, Jack Sadowsky, Brian J. Smith, Peter E. Czabotar, Kimberly J. Peterson‐Kaufman, Peter M. Colman, Samuel H. Gellman, W. Douglas Fairlie,

Tópico(s)

Protein Structure and Dynamics

Resumo

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.

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