Samer Kawak sandbox: Difference between revisions
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==Overview of BAX and Apoptosis== | ==Overview of BAX and Apoptosis== | ||
{{STRUCTURE_1f16 | PDB=1f16 | SCENE= }} | |||
By definition, apoptosis is programmed cell death, or suicide. To induce cell death among cancer cells is a critical component to cancer treatment. Specifically, the Bcl-2 protein family members have been found to have a prominent role in apoptosis, yet researchers have not been able to deduce more information on their mechanisms. Bcl-2 proteins occupy the mitochondrial outer membrane permeabilization, and are recognized either as pro-apoptotic (Bax, BAD, Bak, and Bok) or anti-apoptotic (Bcl-2 proper, Bcl-xL, and Bcl-w). Pro-apoptotic Bcl-2 proteins are death-promoting members while anti-apoptotic members are death-inhibiting structures. Currently, researchers have identified 25 genes in the Bcl-2 family. | By definition, apoptosis is programmed cell death, or suicide. To induce cell death among cancer cells is a critical component to cancer treatment. Specifically, the Bcl-2 protein family members have been found to have a prominent role in apoptosis, yet researchers have not been able to deduce more information on their mechanisms. Bcl-2 proteins occupy the mitochondrial outer membrane permeabilization, and are recognized either as pro-apoptotic (Bax, BAD, Bak, and Bok) or anti-apoptotic (Bcl-2 proper, Bcl-xL, and Bcl-w). Pro-apoptotic Bcl-2 proteins are death-promoting members while anti-apoptotic members are death-inhibiting structures. Currently, researchers have identified 25 genes in the Bcl-2 family. | ||
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==Structure== | ==Structure== | ||
Bax proteins contains 9 alpha helices while alpha-1 through alpha-8 are similar to that of Bcl-xL. The C-terminal alpha-9 helix occupies the hydrophobic pocket, which arbitrates the heterodimer formation and bioactivity of differing members of the Bcl-2 family. Researchers from the 2000 article by Suzuki et al. determined that the Bax structure indicates that the orientation of the alpha-9 helix offers concurrent control over its mitochondrial targeting and dimer formation. | Bax proteins contains 9 alpha helices while alpha-1 through alpha-8 are similar to that of Bcl-xL. The C-terminal alpha-9 helix occupies the hydrophobic pocket, which arbitrates the heterodimer formation and bioactivity of differing members of the Bcl-2 family. Researchers from the 2000 article by Suzuki et al. determined that the Bax structure indicates that the orientation of the alpha-9 helix offers concurrent control over its mitochondrial targeting and dimer formation. | ||
In another article by Gavathiotis et al. (2008), the authors discovered through NMR analysis that the BIM stabilized alpha-helix of Bcl-2 (SAHB) domain binds Bax at an interaction site different from the antiapoptotic proteins. The Bax binding site was also characterized by lysine at <scene name='Samer_Kawak_sandbox/Lys_21/2'>position 21</scene> (K21), glutamine at <scene name='Samer_Kawak_sandbox/Gln_28_and_32/1'>positions 28 and 32</scene> (Q28, Q32), arginine at <scene name='Samer_Kawak_sandbox/Arg_134/1'>position 134</scene> (R134), and glutamic acid at <scene name='Samer_Kawak_sandbox/Glu_131/1'>position 131</scene> (E131). [3] | In another article by Gavathiotis et al. (2008), the authors discovered through NMR analysis that the BIM stabilized alpha-helix of Bcl-2 (SAHB) domain binds Bax at an interaction site different from the antiapoptotic proteins. The Bax binding site was also characterized by lysine at <scene name='Samer_Kawak_sandbox/Lys_21/2'>position 21</scene> (K21), glutamine at <scene name='Samer_Kawak_sandbox/Gln_28_and_32/1'>positions 28 and 32</scene> (Q28, Q32), arginine at <scene name='Samer_Kawak_sandbox/Arg_134/1'>position 134</scene> (R134), and glutamic acid at <scene name='Samer_Kawak_sandbox/Glu_131/1'>position 131</scene> (E131). [3] | ||
[[Image:800px-Signal transduction v1.png|Apoptosis signal pathway| | [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|700 px|thumb]]]] [4] | ||
==Zhang et al. (2000) Study== | ==Zhang et al. (2000) Study== | ||