| The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation. | |
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MedLine Citation:
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PMID: 11427895 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The SAND domain is a conserved sequence motif found in a number of nuclear proteins, including the Sp100 family and NUDR. These are thought to play important roles in chromatin-dependent transcriptional regulation and are linked to many diseases. We have determined the three-dimensional (3D) structure of the SAND domain from Sp100b. The structure represents a novel alpha/beta fold, in which a conserved KDWK sequence motif is found within an alpha-helical, positively charged surface patch. For NUDR, the SAND domain is shown to be sufficient to mediate DNA binding. Using mutational analyses and chemical shift perturbation experiments, the DNA binding surface is mapped to the alpha-helical region encompassing the KDWK motif. The DNA binding activity of wild type and mutant proteins in vitro correlates with transcriptional regulation activity of full length NUDR in vivo. The evolutionarily conserved SAND domain defines a new DNA binding fold that is involved in chromatin-associated transcriptional regulation. |
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Authors:
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M J Bottomley; M W Collard; J I Huggenvik; Z Liu; T J Gibson; M Sattler |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Nature structural biology Volume: 8 ISSN: 1072-8368 ISO Abbreviation: Nat. Struct. Biol. Publication Date: 2001 Jul |
Date Detail:
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Created Date: 2001-06-27 Completed Date: 2001-07-12 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 9421566 Medline TA: Nat Struct Biol Country: United States |
Other Details:
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Languages: eng Pagination: 626-33 Citation Subset: IM |
Affiliation:
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European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/1H5P |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Amino Acid Sequence Animals Antigens, Nuclear* Autoantigens / chemistry*, genetics, metabolism* Base Sequence Binding Sites Cell Line Chromatin / genetics, metabolism Conserved Sequence DNA / genetics, metabolism* DNA-Binding Proteins / chemistry*, genetics, metabolism* Gene Expression Regulation* Genes, Reporter / genetics Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Nuclear Proteins / chemistry*, genetics, metabolism* Point Mutation / genetics Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Static Electricity Transcription, Genetic* |
| Chemical | |
Reg. No./Substance:
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0/Antigens, Nuclear; 0/Autoantigens; 0/Chromatin; 0/DNA-Binding Proteins; 0/Nuclear Proteins; 135844-47-2/Sp100 protein, human; 9007-49-2/DNA |
| Comments/Corrections | |
Comment In:
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Nat Struct Biol. 2001 Jul;8(7):568-70
[PMID:
11427878
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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