Sandbox Reserved 1122: Difference between revisions
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== Structure == | == Structure == | ||
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/ | 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/2'>BH4</scene> (10-30), | ||
<scene name='71/719863/Scenebh3/ | <scene name='71/719863/Scenebh3/3'>BH3</scene> (93-107), <scene name='71/719863/Scenebh1/2'>BH1</scene> (136-155), <scene name='71/719863/Scenebh2/2'>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/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> | 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> | ||
