2imt

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[[Image:2imt.gif|left|200px]]
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{{STRUCTURE_2imt| PDB=2imt | SCENE= }}
{{STRUCTURE_2imt| PDB=2imt | SCENE= }}
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'''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site'''
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===The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17157251 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17157251}}
==About this Structure==
==About this Structure==
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[[Category: Watson, M.]]
[[Category: Watson, M.]]
[[Category: Dimer]]
[[Category: Dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:40:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:59:46 2008''

Revision as of 00:59, 28 July 2008

Image:2imt.png

Template:STRUCTURE 2imt

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

Template:ABSTRACT PUBMED 17157251

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

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