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rdf:type |
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lifeskim:mentions |
umls-concept:C0215508,
umls-concept:C0441655,
umls-concept:C0678594,
umls-concept:C1334043,
umls-concept:C1335654,
umls-concept:C1511545,
umls-concept:C1514562,
umls-concept:C1539715,
umls-concept:C1705326,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2697616
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pubmed:issue |
4
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pubmed:dateCreated |
2006-4-17
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pubmed:abstractText |
AML1/ETO is the chimeric protein resulting from the t(8;21) in acute myeloid leukemia. The Nervy homology 2 (NHR2) domain in ETO mediates oligomerization and AML1/ETO's interactions with ETO, MTGR1, and MTG16, and with the corepressor molecules mSin3A and HDAC1 and HDAC3. We solved the NHR2 domain structure and found it to be an alpha-helical tetramer. We show that oligomerization contributes to AML1/ETO's inhibition of granulocyte differentiation, is essential for its ability to enhance the clonogenic potential of primary mouse bone marrow cells, and affects AML1/ETO's activity on several endogenous genes. Oligomerization is also required for AML1/ETO's interactions with ETO, MTGR1, and MTG16, but not with other corepressor molecules.
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pubmed:grant |
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pubmed:commentsCorrections |
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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 |
1535-6108
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pubmed:author |
pubmed-author:BushwellerJohn HJH,
pubmed-author:CheneyMatthew DMD,
pubmed-author:ChruszczMaksymilianM,
pubmed-author:ColeJamesJ,
pubmed-author:DauterZbyszekZ,
pubmed-author:GaudetJustin JJJ,
pubmed-author:LaryJeffJ,
pubmed-author:LiuYizhouY,
pubmed-author:LukasikStephen MSM,
pubmed-author:MinorWladekW,
pubmed-author:SpeckNancy ANA,
pubmed-author:SugiyamaDaisukeD
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
249-60
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16616331-Amino Acid Sequence,
pubmed-meshheading:16616331-Animals,
pubmed-meshheading:16616331-Binding Sites,
pubmed-meshheading:16616331-Cells, Cultured,
pubmed-meshheading:16616331-Core Binding Factor Alpha 2 Subunit,
pubmed-meshheading:16616331-Crystallography, X-Ray,
pubmed-meshheading:16616331-Gene Expression Regulation,
pubmed-meshheading:16616331-Humans,
pubmed-meshheading:16616331-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16616331-Male,
pubmed-meshheading:16616331-Mice,
pubmed-meshheading:16616331-Mice, Inbred C57BL,
pubmed-meshheading:16616331-Models, Molecular,
pubmed-meshheading:16616331-Molecular Sequence Data,
pubmed-meshheading:16616331-Mutation,
pubmed-meshheading:16616331-Oncogene Proteins, Fusion,
pubmed-meshheading:16616331-Protein Binding,
pubmed-meshheading:16616331-Protein Structure, Quaternary,
pubmed-meshheading:16616331-Sequence Alignment
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pubmed:year |
2006
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pubmed:articleTitle |
The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity.
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pubmed:affiliation |
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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