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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2009-3-2
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pubmed:databankReference |
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pubmed:abstractText |
Interactions of Bcl-2 family proteins play a regulatory role in mitochondrial apoptosis. The pro-apoptotic protein Bak resides in the outer mitochondrial membrane, and the formation of Bak homo- or heterodimers is involved in the regulation of apoptosis. The previously reported structure of the human Bak protein (residues Glu16-Gly186) revealed that a zinc ion was coordinated with two pairs of Asp160 and His164 residues from the symmetry-related molecules. This zinc-dependent homodimer was regarded as an anti-apoptotic dimer. In the present study, we determined the crystal structure of the human Bak residues Ser23-Asn185 at 2.5A, and found a distinct type of homodimerization through Cys166 disulfide bridging between the symmetry-related molecules. In the two modes of homodimerization, the molecular interfaces are completely different. In the membrane-targeted model of the S-S bridged dimer, the BH3 motifs are too close to the membrane to interact directly with the anti-apoptotic relatives, such as Bcl-x(L). Therefore, the Bak dimer structure reported here may represent a pro-apoptotic mode under oxidized conditions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1095-8657
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pubmed:author |
pubmed-author:AkasakaRyogoR,
pubmed-author:ChenLirongL,
pubmed-author:InoueMakotoM,
pubmed-author:KigawaTakanoriT,
pubmed-author:KishishitaSeiichiroS,
pubmed-author:LiuZhi-JieZJ,
pubmed-author:MurayamaKazutakaK,
pubmed-author:ShirouzuMikakoM,
pubmed-author:SuganoSumioS,
pubmed-author:TakemotoChieC,
pubmed-author:TanakaAkikoA,
pubmed-author:TeradaTakahoT,
pubmed-author:Uchikubo-KamoTomomiT,
pubmed-author:WangBi-ChengBC,
pubmed-author:WangHongfeiH,
pubmed-author:YokoyamaShigeyukiS
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pubmed:issnType |
Electronic
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:19135534-Amino Acid Sequence,
pubmed-meshheading:19135534-Crystallization,
pubmed-meshheading:19135534-Crystallography, X-Ray,
pubmed-meshheading:19135534-Cysteine,
pubmed-meshheading:19135534-Cystine,
pubmed-meshheading:19135534-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:19135534-Light,
pubmed-meshheading:19135534-Models, Molecular,
pubmed-meshheading:19135534-Molecular Sequence Data,
pubmed-meshheading:19135534-Molecular Weight,
pubmed-meshheading:19135534-Oxidation-Reduction,
pubmed-meshheading:19135534-Protein Multimerization,
pubmed-meshheading:19135534-Protein Structure, Quaternary,
pubmed-meshheading:19135534-Protein Structure, Tertiary,
pubmed-meshheading:19135534-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:19135534-Recombinant Proteins,
pubmed-meshheading:19135534-Scattering, Radiation,
pubmed-meshheading:19135534-Sequence Homology, Amino Acid,
pubmed-meshheading:19135534-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:19135534-bcl-2 Homologous Antagonist-Killer Protein
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pubmed:year |
2009
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pubmed:articleTitle |
Novel dimerization mode of the human Bcl-2 family protein Bak, a mitochondrial apoptosis regulator.
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pubmed:affiliation |
Systems and Structural Biology Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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