2ims

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(New page: 200px<br /> <applet load="2ims" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ims, resolution 1.48&Aring;" /> '''The X-ray Structure...)
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<applet load="2ims" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2ims, resolution 1.48&Aring;" />
caption="2ims, resolution 1.48&Aring;" />
'''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site'''<br />
'''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site'''<br />
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==About this Structure==
==About this Structure==
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2IMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IMS OCA].
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2IMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMS OCA].
==Reference==
==Reference==
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[[Category: dimer]]
[[Category: dimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:45:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:36:33 2008''

Revision as of 15:36, 15 February 2008


2ims, resolution 1.48Å

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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

2IMS is a Single protein structure of sequence from Homo sapiens with as ligand. 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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