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transmembrane domain (218-239) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure).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). 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 2 isoforms differ from two amino acid but this difference doesn’t induce any change in the conformation of this protein.~~

Bcl-2 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 ~~suppression~~ of the dimerization thus ~~inhibits~~ the activity of Bcl-2.

Bcl-2 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. However as expected, it affect the affinity with Bad and Bak proteins (from the Bcl-2 family). Indeed Bcl-2 isoform 1 shows to have a weaker affinity for Bad and Bak compared to isoform 2.

== Function ==

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 transmembrane domain (218-239) (due to its poor behavior in solution, it has been replaced by a segment of Bcl-xl in the presented 3D structure).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). 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 2 isoforms differ from two amino acid but this difference doesn’t induce any change in the conformation of this protein.
-Bcl-2 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 suppression of the dimerization thus inhibits the activity of Bcl-2.
+Bcl-2 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. However as expected, it affect the affinity with Bad and Bak proteins (from the Bcl-2 family). Indeed Bcl-2 isoform 1 shows to have a weaker affinity for Bad and Bak compared to isoform 2.
 == Function ==