2imt
From Proteopedia
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- | [[Image:2imt.gif|left|200px]] | + | [[Image:2imt.gif|left|200px]] |
- | + | ||
- | '''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site''' | + | {{Structure |
+ | |PDB= 2imt |SIZE=350|CAPTION= <scene name='initialview01'>2imt</scene>, resolution 1.49Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= BAK1, BAK, BCL2L7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2IMT is a [ | + | 2IMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17157251 17157251] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dimer]] | [[Category: dimer]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:31:15 2008'' |
Revision as of 15:31, 20 March 2008
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, resolution 1.49Å | |||||||
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Ligands: | |||||||
Gene: | BAK1, BAK, BCL2L7 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 17:31:15 2008
Categories: Homo sapiens | Single protein | Gehring, K B. | Liu, Q. | Moldoveanu, T. | Shore, G C. | Tocilj, A. | Watson, M. | ZN | Dimer