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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1999-8-6
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pubmed:databankReference |
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pubmed:abstractText |
The core binding factor beta subunit (CBF beta) is the non-DNA binding subunit of the core-binding factors, transcription factors essential for multiple developmental processes including hematopoiesis and bone development. Chromosomal translocations involving the human CBFB gene are associated with a large percentage of human leukemias. The N-terminal 141 amino acids of CBF beta contains the heterodimerization domain for the DNA-binding CBF alpha subunits, and is sufficient for CBF beta function in vivo. Here we present the high-resolution solution structure of the CBF beta heterodimerization domain. It is a novel alpha/beta structure consisting of two three-stranded beta-sheets packed on one another in a sandwich arrangement, with four peripheral alpha-helices. The CBF alpha binding site on CBF beta has been mapped by chemical shift perturbation analysis.
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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 |
Jul
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
624-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10404216-Binding Sites,
pubmed-meshheading:10404216-Circular Dichroism,
pubmed-meshheading:10404216-Core Binding Factor alpha Subunits,
pubmed-meshheading:10404216-Core Binding Factor beta Subunit,
pubmed-meshheading:10404216-DNA-Binding Proteins,
pubmed-meshheading:10404216-Humans,
pubmed-meshheading:10404216-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10404216-Protein Structure, Secondary,
pubmed-meshheading:10404216-Transcription Factor AP-2,
pubmed-meshheading:10404216-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Solution structure of core binding factor beta and map of the CBF alpha binding site.
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pubmed:affiliation |
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville 22906, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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