Source:http://linkedlifedata.com/resource/pfam/family/PF13866.1
Predicate | Object |
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rdf:type | |
family:comment |
SAP30 is a subunit of the histone deacetylase complex, and thisdomain is a zinc-finger. Solution of the structure shows a novel fold comprising two beta-strands and two alpha-helices with the zinc organising centre showing remote resemblance to the treble clef motif. In silico analysis of the structure revealed a highly conserved surface dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 zn-finger motif indicated a strong preference for nucleic acid substrates. The zinc-finger of SAP3 probably functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 co-repressor complex [1].
|
family:id |
zf-SAP30
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family:description |
SAP30 zinc-finger
|
family:authorList |
Coggill P
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family:familyType |
Domain
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family:pubmed | |
family:protein |
http://linkedlifedata.com/resource/pfam/protein/SAP30_HUMAN,
http://linkedlifedata.com/resource/pfam/protein/A8P6G3_BRUMA,
http://linkedlifedata.com/resource/pfam/protein/B7ZSN0_XENTR,
http://linkedlifedata.com/resource/pfam/protein/D3ZC08_RAT,
http://linkedlifedata.com/resource/pfam/protein/S30LA_XENLA
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