2HDE
Solution Structure of Human SAP18
Summary for 2HDE
| Entry DOI | 10.2210/pdb2hde/pdb |
| Descriptor | Histone deacetylase complex subunit SAP18 (1 entity in total) |
| Functional Keywords | hdac, histone deacetylase, sin3, gli, bicoid, gaga, transcriptional repressor, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O00422 |
| Total number of polymer chains | 1 |
| Total formula weight | 16920.24 |
| Authors | McCallum, S.A.,Yin, J.P.,Pan, B.,Fairbrother, W.J. (deposition date: 2006-06-20, release date: 2007-04-24, Last modification date: 2024-05-29) |
| Primary citation | McCallum, S.A.,Bazan, J.F.,Merchant, M.,Yin, J.,Pan, B.,de Sauvage, F.J.,Fairbrother, W.J. Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly. Biochemistry, 45:11974-11982, 2006 Cited by PubMed Abstract: Signal transduction pathways are frequently found to repress transcription of target genes in the absence of stimulation and, conversely, to upregulate transcription in the presence of a signal. Transcription factors are central in this dual regulatory mechanism and widely use a generalized mechanism to repress transcription through recruitment of a Sin3-histone deacetylase (HDAC) complex to their binding sites on DNA. The protein SAP18 (Sin3-associated polypeptide of 18 kDa) has been shown to play a key role in gene-specific recruitment of the HDAC complex by a number of transcription factors including Gli, GAGA, and Bicoid. The solution structure of SAP18 reveals a ubiquitin-like fold with several large loop insertions relative to other family members. This fold supports the functional role of SAP18 as a protein-protein adapter module and provides insight for how SAP18 may bridge the Sin3-HDAC complex to transcription factors. PubMed: 17002296DOI: 10.1021/bi060687l PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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