Peptide name : TO4, human Bax 21-mer (52–72)

Source/Organism : Effectors (BAK, BAX)

Linear/Cyclic : Linear

Chirality : L

Peptide length: 21

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : 24h

Activity : Not found

Cell line : Not found

Cancer type : Not specified

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2336.5756 Dalton

Aliphatic index : 0.790

Instability index : 74.5714

Hydrophobicity (GRAVY) : -0.976

Isoelectric point : 4.8637

Charge (pH 7) : -1.2438

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 0.5

hydrophobic moment : 1.336

Missing amino acid : W,H,P,M,F,Y,N,V

Most occurring amino acid : D

Most occurring amino acid frequency : 3

Least occurring amino acid : Q

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.3, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](N)CCC(N)=O)[C@@H](C)O)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CO)C(=O)O

1 : Diaz JL, et al. A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members. J Biol Chem. 1997; 272:11350-5. doi: 10.1074/jbc.272.17.11350

Paper title : A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members.

Doi : https://doi.org/10.1074/jbc.272.17.11350

Abstract : Bcl-2 inhibits apoptosis induced by a wide variety of stimuli. In contrast, the Bcl-2 homologue, Bax, antagonizes Bcl-2's death protecting function. Bcl-2 forms protein-protein homodimers with itself and heterodimers with Bax, and previous experiments have shown that point mutations in Bcl-2 can abrogate Bax binding while leaving homodimerization intact. These mutagenesis results can be interpreted to suggest that Bcl-2 has separate binding sites that are responsible for homodimer and heterodimer formation. Results from yeast two-hybrid studies have also suggested that homodimerization and heterodimerization reflect distinct modes of interaction. However, using quantitative plate binding assays, we now show that Bax as well as peptides derived from the BH3 domains of Bax and Bak block both Bcl-2/Bax binding and Bcl-2/Bcl-2 binding. Similar assays demonstrate that Bcl-xL can form both homodimers and heterodimers and that these interactions are also inhibited by Bax and the BH3-derived peptides. These results demonstrate that the same binding motifs are responsible for both homodimerization and heterodimerization of Bcl-2 family members.