1s5r: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1s5r.jpg|left|200px]] | [[Image:1s5r.jpg|left|200px]] | ||
'''Solution Structure of HBP1 SID-mSin3A PAH2 Complex''' | {{Structure | ||
|PDB= 1s5r |SIZE=350|CAPTION= <scene name='initialview01'>1s5r</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= Sin3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''Solution Structure of HBP1 SID-mSin3A PAH2 Complex''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1S5R is a [ | 1S5R is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5R OCA]. | ||
==Reference== | ==Reference== | ||
HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations., Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I, Nat Struct Mol Biol. 2004 Aug;11(8):738-46. Epub 2004 Jul 4. PMID:[http:// | HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations., Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I, Nat Struct Mol Biol. 2004 Aug;11(8):738-46. Epub 2004 Jul 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15235594 15235594] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 26: | Line 35: | ||
[[Category: repressor-corepressor complex]] | [[Category: repressor-corepressor complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:55 2008'' | ||
Revision as of 15:00, 20 March 2008
| |||||||
| Gene: | Sin3A (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of HBP1 SID-mSin3A PAH2 Complex
OverviewOverview
Recruitment of the histone deacetylase (HDAC)-associated Sin3 corepressor is an obligatory step in many eukaryotic gene silencing pathways. Here we show that HBP1, a cell cycle inhibitor and regulator of differentiation, represses transcription in a HDAC/Sin3-dependent manner by targeting the mammalian Sin3A (mSin3A) PAH2 domain. HBP1 is unrelated to the Mad1 repressor for which high-resolution structures in complex with PAH2 have been described. We show that like Mad1, the HBP1 transrepression domain binds through a helical structure to the hydrophobic cleft of mSin3A PAH2. Notably, the HBP1 helix binds PAH2 in a reversed orientation relative to Mad1 and, equally unexpectedly, this is correlated with a chain reversal of the minimal Sin3 interaction motifs. These results not only provide insights into how multiple, unrelated transcription factors recruit the same coregulator, but also have implications for how sequence similarity searches are conducted.
About this StructureAbout this Structure
1S5R is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations., Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I, Nat Struct Mol Biol. 2004 Aug;11(8):738-46. Epub 2004 Jul 4. PMID:15235594
Page seeded by OCA on Thu Mar 20 14:00:55 2008