2imt
From Proteopedia
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|PDB= 2imt |SIZE=350|CAPTION= <scene name='initialview01'>2imt</scene>, resolution 1.49Å | |PDB= 2imt |SIZE=350|CAPTION= <scene name='initialview01'>2imt</scene>, resolution 1.49Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= BAK1, BAK, BCL2L7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= BAK1, BAK, BCL2L7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1maz|1MAZ]], [[1f16|1F16]], [[1lxl|1LXL]], [[1bxl|1BXL]], [[1mk3|1MK3]], [[1wsx|1WSX]], [[2ims|2IMS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2imt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imt OCA], [http://www.ebi.ac.uk/pdbsum/2imt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2imt RCSB]</span> | ||
}} | }} | ||
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[[Category: Tocilj, A.]] | [[Category: Tocilj, A.]] | ||
[[Category: Watson, M.]] | [[Category: Watson, M.]] | ||
| - | [[Category: ZN]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:46:14 2008'' |
Revision as of 00:46, 31 March 2008
| |||||||
| , resolution 1.49Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BAK1, BAK, BCL2L7 (Homo sapiens) | ||||||
| Related: | 1MAZ, 1F16, 1LXL, 1BXL, 1MK3, 1WSX, 2IMS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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