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) (not present in the presented 3D structure because of the poor behaviour in solution of the protein containing the transmembrane region). 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) and 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) (not present in the presented 3D structure because of the poor behaviour in solution of the protein containing the transmembrane region). 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) and there are also 3 turns (32-34, 123-125, 138-140). The <scene name='71/719863/Bcl2helix/2'>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>


Helices 5 and 6 are mostly hydrophobic and they are surrounded by four other helices characterized by their amphipathic properties. This type of structure with alpha-helices is also encountered in some bacterial toxins such as diphteria toxin where it permits to form pores in membranes. This similarity of arrangement suggests that Bcl-2, as well as diphteria toxin, is able to interfere in permeability of organelles like endoplasmic reticulum or mitochondria. <ref>[https://books.google.fr/books?id=WhwvPX0K2BMC&pg=PA36&lpg=PA36&dq=bcl-2+isoform+1+electrostatic+potential&source=bl&ots=y3NzAJJIuV&sig=hlbn50xllAZ7fArKAODsypZZD1A&hl=fr&sa=X&ved=0ahUKEwjS88_0ztHKAhWH0hoKHddyAdIQ6AEIQTAD#v=onepage&q=bcl-2%20isoform%201%20electrostatic%20potential&f=false  
Helices 5 and 6 are mostly hydrophobic and they are surrounded by four other helices characterized by their amphipathic properties. This type of structure with alpha-helices is also encountered in some bacterial toxins such as diphteria toxin where it permits to form pores in membranes. This similarity of arrangement suggests that Bcl-2, as well as diphteria toxin, is able to interfere in permeability of organelles like endoplasmic reticulum or mitochondria. <ref>[https://books.google.fr/books?id=WhwvPX0K2BMC&pg=PA36&lpg=PA36&dq=bcl-2+isoform+1+electrostatic+potential&source=bl&ots=y3NzAJJIuV&sig=hlbn50xllAZ7fArKAODsypZZD1A&hl=fr&sa=X&ved=0ahUKEwjS88_0ztHKAhWH0hoKHddyAdIQ6AEIQTAD#v=onepage&q=bcl-2%20isoform%201%20electrostatic%20potential&f=false  
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