|
|||||
|
|
High‐Resolution Structural Characterization of a Helical α/β‐Peptide Foldamer Bound to the Anti‐Apoptotic Protein Bcl‐xL |
|
| Authors: | Erinna?F Lee Dr Jack?D Sadowsky Brian?J Smith Dr Peter?E Czabotar Dr Kimberly?J Peterson‐Kaufman Peter?M Colman Prof Samuel?H Gellman Prof W?Douglas Fairlie Dr |
| Institution: | 1. Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3052 (Australia), Fax: (+61)?3‐9345‐2686;2. These authors contributed equally.;3. Department of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, WI 53706 (USA), Fax: (+1)?608‐265‐4534 |
| 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 α‐ and β‐amino acid residues and is bound to the anti‐apoptotic protein Bcl‐xL. The overall binding mode and key interactions observed in the foldamer/Bcl‐xL complex mimic those seen in complexes of Bcl‐xL with natural α‐peptide ligands. Additional contacts in the foldamer/Bcl‐xL complex involving β‐amino acid residues appear to contribute to binding affinity.  |
| Keywords: | amino acids foldamers peptides protein– protein interactions X‐ray diffraction |