2YJ1
Puma BH3 foldamer in complex with Bcl-xL
Summary for 2YJ1
| Entry DOI | 10.2210/pdb2yj1/pdb |
| Related | 1BXL 1G5J 1LXL 1MAZ 1R2D 1R2E 1R2G 1R2H 1R2I 1YSG 1YSI 1YSN 2B48 |
| Descriptor | BCL-2-LIKE PROTEIN 1, ALPHA-BETA-PUMA BH3 FOLDAMER (3 entities in total) |
| Functional Keywords | apoptosis, membrane protein, foldamer, bh3 domain, autophagy |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 41069.87 |
| Authors | Lee, E.F.,Smith, B.J.,Horne, W.S.,Mayer, K.N.,Evangelista, M.,Colman, P.M.,Gellman, S.H.,Fairlie, W.D. (deposition date: 2011-05-18, release date: 2011-10-12, Last modification date: 2024-05-15) |
| Primary citation | Lee, E.F.,Smith, B.J.,Horne, W.S.,Mayer, K.N.,Evangelista, M.,Colman, P.M.,Gellman, S.H.,Fairlie, W.D. Structural Basis of Bcl-Xl Recognition by a Bh3-Mimetic Alpha-Beta-Peptide Generated Via Sequence-Based Design Chembiochem, 12:2025-, 2011 Cited by PubMed Abstract: The crystal structure of a complex between the prosurvival protein Bcl-x(L) and an α/β-peptide 21-mer is described. The α/β-peptide contains six β-amino acid residues distributed periodically throughout the sequence and adopts an α-helix-like conformation that mimics the bioactive shape of the Puma BH3 domain. The α/β-peptide forms all of the noncovalent contacts that have previously been identified as necessary for recognition of the prosurvival protein by an authentic BH3 domain. Comparison of our α/β-peptide:Bcl-x(L) structure with structures of complexes between native BH3 domains and Bcl-2 family proteins reveals how subtle adjustments, including variations in helix radius and helix bowing, allow the α/β-peptide to engage Bcl-x(L) with high affinity. Geometric comparisons of the BH3-mimetic α/β-peptide with α/β-peptides in helix-bundle assemblies provide insight on the conformational plasticity of backbones that contain combinations of α- and β-amino acid residues. The BH3-mimetic α/β-peptide displays prosurvival protein-binding preferences distinct from those of Puma BH3 itself, even though these two oligomers have identical side-chain sequences. Our results suggest origins for this backbone-dependent change in selectivity. PubMed: 21744457DOI: 10.1002/CBIC.201100314 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.24 Å) |
Structure validation
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