Sandbox Reserved 1122: Difference between revisions
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The transmembrane domain of Bcl-2 is made of 21 aminoacids and is located at the carboxy-terminal tail of the protein. It allows the docking of Bcl-2 in the mitochondrial outer membrane where the protein interacts with other effectors.<ref>[http://www.ncbi.nlm.nih.gov/pubmed/24905660 Peptides derived from the transmembrane domain of Bcl-2 proteins as potential mitochondrial priming tools.]</ref> | The transmembrane domain of Bcl-2 is made of 21 aminoacids and is located at the carboxy-terminal tail of the protein. It allows the docking of Bcl-2 in the mitochondrial outer membrane where the protein interacts with other effectors.<ref>[http://www.ncbi.nlm.nih.gov/pubmed/24905660 Peptides derived from the transmembrane domain of Bcl-2 proteins as potential mitochondrial priming tools.]</ref> | ||
The tertiary structure of Bcl-2 shows that this protein contains a hydrophobic groove on its surface that allows dimerization with other members of the Bcl-2 family. This region needs to be highly conserved to keep the ability of interacting with proapoptotic protein of the family, in fact, it has been shown that a mutation in this structure leads to the silencing of the dimerization thus may inhibit the activity of Bcl-2. | The tertiary structure of Bcl-2 shows that this protein contains a hydrophobic groove on its surface that allows dimerization with other members of the Bcl-2 family. This region needs to be highly conserved to keep the ability of interacting with the BH3 domain of the proapoptotic protein of the family, in fact, it has been shown that a mutation in this structure leads to the silencing of the dimerization thus may inhibit the activity of Bcl-2. | ||
The isoform 1 and 2 differs from two amino acid in the hydrophobic groove but this difference doesn’t induce any change in the conformation of this protein. | The isoform 1 and 2 differs from two amino acid in the hydrophobic groove but this difference doesn’t induce any change in the conformation of this protein. | ||
However as expected, it affect the affinity with Bad and Bak proteins (from the Bcl-2 family). Indeed Bcl-2 isoform 1 shows to have a weaker affinity for Bad and Bak compared to isoform 2.<ref>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC30598/ Solution structure of the antiapoptotic protein bcl-2]</ref> | However as expected, it affect the affinity with Bad and Bak proteins (from the Bcl-2 family). Indeed Bcl-2 isoform 1 shows to have a weaker affinity for Bad and Bak compared to isoform 2.<ref>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC30598/ Solution structure of the antiapoptotic protein bcl-2]</ref> | ||
