Sandbox Reserved 1122: Difference between revisions
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Human Bcl-2, isoform 1 is a 26kDa protein of 239 residues which is negatively charged at pH 7. The linear structure highlights 5 domains: <scene name='71/719863/Scenelucas/1'>BH4</scene> (10-30), | Human Bcl-2, isoform 1 is a 26kDa protein of 239 residues which is negatively charged at pH 7. The linear structure highlights 5 domains: <scene name='71/719863/Scenelucas/1'>BH4</scene> (10-30), | ||
<scene name='71/719863/Scenebh3/2'>BH3</scene> (93-107), <scene name='71/719863/Scenebh1/1'>BH1</scene> (136-155), <scene name='71/719863/Scenebh2/1'>BH2</scene> (187-202) and a | <scene name='71/719863/Scenebh3/2'>BH3</scene> (93-107), <scene name='71/719863/Scenebh1/1'>BH1</scene> (136-155), <scene name='71/719863/Scenebh2/1'>BH2</scene> (187-202) and a | ||
transmembrane domain (212-233) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure).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 (α1) , from 93 to 107 (α2), from 109 to 118 (α3), from 126 to 137 (α4), from 144-163 (α5), from 169 to 184 (α6), from 186 to 191 (α7) and from 194 to 202(α8). 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 | transmembrane domain (212-233) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure).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 (α1) , from 93 to 107 (α2), from 109 to 118 (α3), from 126 to 137 (α4), from 144-163 (α5), from 169 to 184 (α6), from 186 to 191 (α7) and from 194 to 202 (α8). 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 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 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> | ||
