pubmed-article:19135534 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C1564881 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:19135534 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
pubmed-article:19135534 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:19135534 | pubmed:dateCreated | 2009-3-2 | lld:pubmed |
pubmed-article:19135534 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | 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. | lld:pubmed |
pubmed-article:19135534 | pubmed:language | eng | lld:pubmed |
pubmed-article:19135534 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19135534 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19135534 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19135534 | pubmed:month | Apr | lld:pubmed |
pubmed-article:19135534 | pubmed:issn | 1095-8657 | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:SuganoSumioS | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:InoueMakotoM | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:KigawaTakanor... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:YokoyamaShige... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:ShirouzuMikak... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:TanakaAkikoA | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:TeradaTakahoT | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:KishishitaSei... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:LiuZhi-JieZJ | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:WangBi-ChengB... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:ChenLirongL | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:MurayamaKazut... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:WangHongfeiH | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:Uchikubo-Kamo... | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:AkasakaRyogoR | lld:pubmed |
pubmed-article:19135534 | pubmed:author | pubmed-author:TakemotoChieC | lld:pubmed |
pubmed-article:19135534 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19135534 | pubmed:volume | 166 | lld:pubmed |
pubmed-article:19135534 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19135534 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19135534 | pubmed:pagination | 32-7 | lld:pubmed |
pubmed-article:19135534 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:19135534 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19135534 | pubmed:articleTitle | Novel dimerization mode of the human Bcl-2 family protein Bak, a mitochondrial apoptosis regulator. | lld:pubmed |
pubmed-article:19135534 | pubmed:affiliation | Systems and Structural Biology Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan. | lld:pubmed |
pubmed-article:19135534 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19135534 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:578 | entrezgene:pubmed | pubmed-article:19135534 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19135534 | lld:entrezgene |