2imt
From Proteopedia
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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''' | ||
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[[Category: Tocilj, A.]] | [[Category: Tocilj, A.]] | ||
[[Category: Watson, M.]] | [[Category: Watson, M.]] | ||
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Revision as of 04:40, 4 May 2008
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.
About this Structure
2IMT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site., Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K, Mol Cell. 2006 Dec 8;24(5):677-88. PMID:17157251 Page seeded by OCA on Sun May 4 07:40:17 2008
