Sandbox Reserved 1122: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
transmembrane domain (212-233) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure).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. <ref>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC30598/ Solution structure of the antiapoptotic protein bcl-2]</ref> | transmembrane domain (212-233) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure).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. <ref>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC30598/ Solution structure of the antiapoptotic protein bcl-2]</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 membrane of cellular organelles especially mitochondria and endoplasmic reticulum. | 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 membrane of cellular organelles especially mitochondria and endoplasmic reticulum. The localization at the membrane permits an efficient interaction with 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 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 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. | ||
