2ims: Difference between revisions

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[[Image:2ims.~~jpg~~|left|200px]]

[[Image:2ims.png|left|200px]]

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~~'''~~The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site~~'''~~

===The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site===

~~==Overview==~~

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~~BAK/BAX~~-~~mediated mitochondrial outer~~-~~membrane permeabilization (MOMP) drives cell death during development and tissue homeostasis from zebrafish to humans. In most cancers~~, ~~this pathway is inhibited by BCL-2 family antiapoptotic members~~, ~~which bind and block~~ the ~~action of proapoptotic BCL proteins. We report~~ the ~~1.5 A crystal structure of calpain-proteolysed BAK, cBAK, to reveal a zinc binding site that regulates its activity via homodimerization~~. ~~cBAK contains an occluded BH3 peptide binding pocket that binds a BID BH3 peptide only weakly~~ . ~~Nonetheless~~, ~~cBAK requires activation by truncated BID to induce cytochrome c release in mitochondria isolated from bak/bax double-knockout mouse embryonic fibroblasts~~. ~~The BAK~~-~~mediated MOMP is inhibited by low micromolar zinc levels. This inhibition is alleviated by mutation of the zinc~~-~~coordination site in BAK. Our results link directly the antiapoptotic effects of zinc to BAK.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17157251}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17157251 is the PubMed ID number.

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==About this Structure==

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[[Category: Watson, M.]]

[[Category: Dimer]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 07~~:40:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:18:26 2008''

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-[[Image:2ims.jpg|left|200px]]
+{{Seed}}
+[[Image:2ims.png|left|200px]]
 <!--
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 {{STRUCTURE_2ims|  PDB=2ims  |  SCENE=  }}
-'''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site'''
+===The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site===
-==Overview==
+<!--
-BAK/BAX-mediated mitochondrial outer-membrane permeabilization (MOMP) drives cell death during development and tissue homeostasis from zebrafish to humans. In most cancers, this pathway is inhibited by BCL-2 family antiapoptotic members, which bind and block the action of proapoptotic BCL proteins. We report the 1.5 A crystal structure of calpain-proteolysed BAK, cBAK, to reveal a zinc binding site that regulates its activity via homodimerization. cBAK contains an occluded BH3 peptide binding pocket that binds a BID BH3 peptide only weakly . Nonetheless, cBAK requires activation by truncated BID to induce cytochrome c release in mitochondria isolated from bak/bax double-knockout mouse embryonic fibroblasts. The BAK-mediated MOMP is inhibited by low micromolar zinc levels. This inhibition is alleviated by mutation of the zinc-coordination site in BAK. Our results link directly the antiapoptotic effects of zinc to BAK.
+The line below this paragraph, {{ABSTRACT_PUBMED_17157251}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17157251 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17157251}}
 ==About this Structure==
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 [[Category: Watson, M.]]
 [[Category: Dimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:40:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:18:26 2008''