Sandbox Reserved 1122: Difference between revisions
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transmembrane domain (218-239) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure). It organizes as eight alpha-helices: from 11 to 25 (1) , from 93 to 107 (2), from 109 to 118 (3), from 126 to 137 (4), from 144-163 (5), from 169 to 184 (6), from 186 to 191 (7) and from 194 to 202(8). Helices 5 and 6 are mostly hydrophobic and they are surrounded by four other helices characterized by their amphipathic properties. There are also 3 turns (32-34, 123-125, 138-140). The <scene name='71/719863/Bcl2helix/1'>3rd alpha-helix</scene> is a 3(10) helix, whereas BCL-XL 3rd helix is a normal alpha-helix. | transmembrane domain (218-239) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure). It organizes as eight alpha-helices: from 11 to 25 (1) , from 93 to 107 (2), from 109 to 118 (3), from 126 to 137 (4), from 144-163 (5), from 169 to 184 (6), from 186 to 191 (7) and from 194 to 202(8). Helices 5 and 6 are mostly hydrophobic and they are surrounded by four other helices characterized by their amphipathic properties. There are also 3 turns (32-34, 123-125, 138-140). The <scene name='71/719863/Bcl2helix/1'>3rd alpha-helix</scene> is a 3(10) helix, whereas BCL-XL 3rd helix is a normal alpha-helix. | ||
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. | 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 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. | ||
